(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIJ0_GEOS0

ID   A0A0F6BIJ0_GEOS0        Unreviewed;       245 AA.
AC   A0A0F6BIJ0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 29.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658, ECO:0000256|SAAS:SAAS00727989};
DE            EC=5.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658, ECO:0000256|SAAS:SAAS00015920};
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000256|HAMAP-Rule:MF_01014};
GN   Name=hisA {ECO:0000256|HAMAP-Rule:MF_01014};
GN   OrderedLocusNames=GY4MC1_0400 {ECO:0000313|EMBL:ADP73241.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73241.1};
RN   [1] {ECO:0000313|EMBL:ADP73241.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73241.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC         phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC         ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01014,
CC         ECO:0000256|RuleBase:RU003658, ECO:0000256|SAAS:SAAS01118349};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658,
CC       ECO:0000256|SAAS:SAAS00015865}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003658, ECO:0000256|SAAS:SAAS00345444}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000256|HAMAP-
CC       Rule:MF_01014, ECO:0000256|RuleBase:RU003657,
CC       ECO:0000256|SAAS:SAAS00541187}.
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DR   EMBL; CP002293; ADP73241.1; -; Genomic_DNA.
DR   RefSeq; WP_003248074.1; NC_014650.1.
DR   EnsemblBacteria; ADP73241; ADP73241; GY4MC1_0400.
DR   GeneID; 29236942; -.
DR   KEGG; gmc:GY4MC1_0400; -.
DR   KO; K01814; -.
DR   OMA; EWLHLVD; -.
DR   OrthoDB; 794219at2; -.
DR   BioCyc; GSP581103:G1GOQ-445-MONOMER; -.
DR   UniPathway; UPA00031; UER00009.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04732; HisA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01014; HisA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR006063; HisA.
DR   InterPro; IPR023016; Isoase_HisA-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00007; TIGR00007; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIJ0.
DR   SWISS-2DPAGE; A0A0F6BIJ0.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01014,
KW   ECO:0000256|RuleBase:RU003657, ECO:0000256|SAAS:SAAS00015854};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658,
KW   ECO:0000256|SAAS:SAAS00423700};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01014,
KW   ECO:0000256|RuleBase:RU003657, ECO:0000256|SAAS:SAAS00423728};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658,
KW   ECO:0000256|SAAS:SAAS00423732, ECO:0000313|EMBL:ADP73241.1}.
FT   ACT_SITE        11
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   245 AA;  26021 MW;  FB23595DBB44C442 CRC64;
     MAAFTIYPAI DIRGGKCVRL LQGDYTKETV YGDSPVEMAA LFAEQGAEWI HMVDLDGAKE
     GKRVNDRFVV EAAKQLPVKV QIGGGIRTED DIVYYLENGV ARVILGSAAI ARPSFVKEML
     KKYGERIAIG IDAKDGFVAT EGWLHTSNVK ATDLGKELAE AGAQTFIFTD IATDGMLSGP
     NIQAAVEMAR ATGKDVIASG GVRSLADLVS LQNHVGDGVA GAIVGKALYT KQFTVAEALK
     VVQGE
//

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