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Database: UniProt
Entry: N1Z561_9CLOT
LinkDB: N1Z561_9CLOT
Original site: N1Z561_9CLOT 
ID   N1Z561_9CLOT            Unreviewed;       238 AA.
AC   N1Z561;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|ARBA:ARBA00018464, ECO:0000256|HAMAP-Rule:MF_01014};
DE            EC=5.3.1.16 {ECO:0000256|ARBA:ARBA00012550, ECO:0000256|HAMAP-Rule:MF_01014};
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   ECO:0000313|EMBL:USF30070.1};
GN   ORFNames=C820_001494 {ECO:0000313|EMBL:USF30070.1}, C820_02606
GN   {ECO:0000313|EMBL:EMZ10946.1};
OS   Clostridium sp. MD294.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ10946.1};
RN   [1] {ECO:0000313|EMBL:EMZ10946.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF356 {ECO:0000313|EMBL:EMZ10946.1};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
RN   [2] {ECO:0000313|EMBL:USF30070.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASF356 {ECO:0000313|EMBL:USF30070.1};
RA   Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA   Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT   "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT   Model to Study Microbiome Function.";
RL   Submitted (MAY-2022) 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|ARBA:ARBA00000901, ECO:0000256|HAMAP-
CC         Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
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|ARBA:ARBA00005133, ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003658}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003658}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003657}.
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DR   EMBL; AQFQ01000029; EMZ10946.1; -; Genomic_DNA.
DR   EMBL; CP097810; USF30070.1; -; Genomic_DNA.
DR   RefSeq; WP_004038410.1; NZ_VIRC01000023.1.
DR   AlphaFoldDB; N1Z561; -.
DR   STRING; 97138.C820_02606; -.
DR   PATRIC; fig|97138.3.peg.2615; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_1_9; -.
DR   OrthoDB; 9807749at2; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000012445; Chromosome.
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; Aldolase class I; 1.
DR   HAMAP; MF_01014; HisA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR006063; HisA_bact_arch.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR023016; Isoase_HisA-like_bact.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00007; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; 1.
DR   PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   PANTHER; PTHR43090:SF2; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01014};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01014};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012445}.
FT   ACT_SITE        8
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   238 AA;  25678 MW;  704F6E54E5509232 CRC64;
     MQIYAAVDIK NGKCVRLKQG KFDDVTVYEQ NPVKAAQNWI QKGASYLHIV DLDGAKQGIS
     QNEQILEEIV KLSDVPVQTG GGVRSLEDIQ RKLLKGVSRV ILGTVAVKQP LLVKQAVEKF
     GADSIVVGID AKNGNVAVAG WEEVSNVSAL ELCLQMKEYG VKTVIYTDIA KDGMMSGGNV
     EATKELVDKT GMDIIASGGI SSMQDLENVK NINVQGVIVG KALYQGVLDL TEIVKKFE
//
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