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UXAC_BACP2
ID   UXAC_BACP2              Reviewed;         478 AA.
AC   A8FHC4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Uronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
DE            EC=5.3.1.12 {ECO:0000255|HAMAP-Rule:MF_00675};
DE   AltName: Full=Glucuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
DE   AltName: Full=Uronic isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
GN   Name=uxaC {ECO:0000255|HAMAP-Rule:MF_00675}; OrderedLocusNames=BPUM_2987;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucuronate = D-fructuronate; Xref=Rhea:RHEA:13049,
CC         ChEBI:CHEBI:58720, ChEBI:CHEBI:59863; EC=5.3.1.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00675};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-galacturonate = keto-D-tagaturonate;
CC         Xref=Rhea:RHEA:27702, ChEBI:CHEBI:12952, ChEBI:CHEBI:17886;
CC         EC=5.3.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00675};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000255|HAMAP-Rule:MF_00675}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Uronate isomerase family. {ECO:0000255|HAMAP-Rule:MF_00675}.
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DR   EMBL; CP000813; ABV63641.1; -; Genomic_DNA.
DR   RefSeq; WP_012011237.1; NZ_VEIS01000008.1.
DR   AlphaFoldDB; A8FHC4; -.
DR   SMR; A8FHC4; -.
DR   STRING; 315750.BPUM_2987; -.
DR   PRIDE; A8FHC4; -.
DR   EnsemblBacteria; ABV63641; ABV63641; BPUM_2987.
DR   KEGG; bpu:BPUM_2987; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_9; -.
DR   OMA; IWHQCNE; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR   HAMAP; MF_00675; UxaC; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR003766; Uronate_isomerase.
DR   Pfam; PF02614; UxaC; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..478
FT                   /note="Uronate isomerase"
FT                   /id="PRO_1000061949"
SQ   SEQUENCE   478 AA;  55773 MW;  A3595574FC38C245 CRC64;
     MKAFLNEQFL LNSPTAEKLY HEFAKDLPII DYHCHLSPKD IYENKTFRNI TEAWLYGDHY
     KWRAMRANGI PETHVTGDAS DYDKFLAWAK TVPMTIGNPL YHWTHLELRR YFEVQDLLNE
     KNADTIWQKV NEKLQEEGFG ARDFIMKSNV ETVVTTDDPI DSLQYHQKLR EEGFSVQVLP
     GFRPDKALDI ANDLFEKYVH ELAEASAISI QSYQDFLNAL RARIDFFHEH GCLISDHAIN
     EMTYEETTQE EVETIFHKRM SGYPLTEKEK IKFKTETFIM LGQAYCERGW AMQLHINALR
     NNNTKMFERL GPDTGYDAMN DEDIAKPLCR ILDRLEQEDA LPNTILYSLN PRDNVVISTL
     AGSFQDGKTP GKMQHGTAWW FNDTKQGMTE QMMTLSSIGL ISRFIGMLTD SRSFLSYTRH
     EYFRRLLCDI IGDWVEKGEV PYDLELLGEI VKGISYENAK QYFQFDRVKQ LHHQSKIT
 
 
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