ID A0A0G3HJW3_9CORY Unreviewed; 243 AA.
AC A0A0G3HJW3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|HAMAP-Rule:MF_01014};
DE EC=5.3.1.16 {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:AKK11417.1};
GN ORFNames=CUTER_07140 {ECO:0000313|EMBL:AKK11417.1};
OS Corynebacterium uterequi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK11417.1, ECO:0000313|Proteomes:UP000035548};
RN [1] {ECO:0000313|EMBL:AKK11417.1, ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|EMBL:AKK11417.1,
RC ECO:0000313|Proteomes:UP000035548};
RX PubMed=26227590;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Virulence Factor Genes Detected in the Complete Genome Sequence of
RT Corynebacterium uterequi DSM 45634, Isolated from the Uterus of a Maiden
RT Mare.";
RL Genome Announc. 3:e00783-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium uterequi DSM 45634, isolated
RT from the uterus of a maiden mare.";
RL Submitted (MAY-2015) 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};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01014}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01014,
CC ECO:0000256|RuleBase:RU003657}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011546; AKK11417.1; -; Genomic_DNA.
DR RefSeq; WP_047259837.1; NZ_CP011546.1.
DR AlphaFoldDB; A0A0G3HJW3; -.
DR STRING; 1072256.CUTER_07140; -.
DR KEGG; cut:CUTER_07140; -.
DR PATRIC; fig|1072256.5.peg.1412; -.
DR OrthoDB; 9807749at2; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000035548; 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:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:InterPro.
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; IPR010188; HisA/PriA_Actinobacteria.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR023016; Isoase_HisA-like_bact.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR01919; hisA-trpF; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014};
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:UP000035548}.
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ SEQUENCE 243 AA; 25705 MW; D3D0B7456ECFE92D CRC64;
MTFTLLPAVD VVNGQAVRLN KGEAGTEKSY GTPLDAALTW QEQGAQWLHF VDLDAAFGRG
SNHELMAEIT GRLDIKVELT GGIRDDESLE RALGTGAARV NIGTAALQRP EWIAGVLARY
PEQVAVDLAV LADGDTLRVK GNGWVSDGGD LWEVLERLDA AGCQRFVVTD VSKDGTLAGP
NIELLRDVSA ATDAAVTASG GISNLADVEQ VARYADEGID SVIIGKALYE RRFTLAEALA
AVA
//