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Description:
Probable phosphoacetylglucosamine mutase (EC 5.4.2.3) (PAGM)(Acetylglucosamine phosphomutase) (N-acetylglucosamine-phosphatemutase) (DNA-damage-repair/toleration protein DRT101).
Molecular weight: 60391
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 1.
07-MAR-2006, entry version 34.
Phylogenetic order:
Eukaryota Viridiplantae Streptophyta Embryophyta Tracheophyta Spermatophyta Magnoliophyta eudicotyledons core eudicotyledons rosids eurosids II Brassicales Brassicaceae Arabidopsis.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein AGM1_ARATH:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AB012246 | BAB09465.1 | - |
| EMBL | AY075620 | AAL91631.1 | - |
| EMBL | L11367 | AAA72352.1 | ALT_SEQ |
| GenomeReviews | BA000015_GR | AT5G18070.1 | |
| TAIR | At5g18070 | -.1 | |
| InterPro | IPR005841 | PG/PMM_mutase. | |
| InterPro | IPR005844 | PG_PMM_ABAI. | |
| InterPro | IPR005843 | PG_PMM_C. | |
| Pfam | PF02878 | PGM_PMM_I | 1. |
| Pfam | PF00408 | PGM_PMM_IV | 1. |
| PROSITE | PS00710 | PGM_PMM | FALSE_NEG. |
Keywords:
DNA damage; DNA repair; Isomerase; Magnesium; Metal-binding; Phosphorylation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=98403884; PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI.
RT Sequence features of the regions of 1,367,185 bp covered by 19
RT physically assigned P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 183-556.
RC STRAIN=cv. Columbia;
RX MEDLINE=93320380; PubMed=8329681;
RA Pang Q., Hays J.B., Rajagopal I., Schaefer T.S.;
RT "Selection of Arabidopsis cDNAs that partially correct phenotypes of
RT Escherichia coli DNA-damage-sensitive mutants and analysis of two
RT plant cDNAs that appear to express UV-specific dark repair
RT activities.";
RL Plant Mol. Biol. 22:411-426(1993).
Feature:
CHAIN 1 556 Probable phosphoacetylglucosamine mutase.
/FTId=PRO_0000148015.
ACT_SITE 68 68 Phosphoserine intermediate (By
similarity).
METAL 68 68 Magnesium (via phosphate group) (By
similarity).
METAL 286 286 Magnesium (By similarity).
METAL 288 288 Magnesium (By similarity).
METAL 290 290 Magnesium (By similarity).
Comments:
-!- FUNCTION: Interconverts GlcNAc-6-P and GlcNAc-1-P (By similarity).
-!- CATALYTIC ACTIVITY: N-acetyl-alpha-D-glucosamine 1-phosphate = N-
acetyl-D-glucosamine 6-phosphate.
-!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
-!- PATHWAY: UDP-GlcNAc biosynthesis from Fru-6-P; third step.
-!- SIMILARITY: Belongs to the phosphohexose mutase family.
-!- CAUTION: Ref.3 sequence differs from that shown due to several
sequencing problems.
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Sequence length: 556
MDEIQIASIL KSSELFPIPQ GVKLSYGTAG FRGDAKLLES TVYRVGILSA LRSLKLGSAT
VGLMITASHN KVSDNGIKVS DPSGFMLSQE WEPFADQIAN ASSPEELVSL IRKFMEKEEI
AIGENNKGAE VWLGRDTRPS GESLLRAGEI GVGSILGSVA IDIGILTTPQ LHWMVRAKNK
GLKATENDYF ENLSTSFRCL IDLIPSSGND KLEISKLLVD GANGVGGQKI EKLRGSLSNL
DVEIRNTGRD GGVLNEGVGA DFVQKEKVLP VGFGFKDVGM RCASLDGDAD RLVYFYIPSD
SSEKVELLDG DKILSLFALF IKEQLNALED DEERKQSRLG VVQTAYANGA STDYLKHLGL
DVVFAKTGVK HLHEKAAEFD IGIYFEANGH GTILFSESFL SWLVSKQKDL TAKGQGGSEE
HKAVSRLMAV SNLINQAVGD ALSGVLLVEV ILQHLGWSIE KWNELYKDLP SRQIKVEVPD
RTAVVTTSEE TEALRPMGIQ DAINSEIKKY SRGRAFIRPS GTEDVVRVYA EASTQEDADS
LANSVAQLVK SFLGSS