ID A0A177NCB7_9GAMM Unreviewed; 247 AA.
AC A0A177NCB7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
DE EC=5.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01014, ECO:0000256|RuleBase:RU003658};
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 ORFNames=A1356_09035 {ECO:0000313|EMBL:OAI27476.1}, A1507_12720
GN {ECO:0000313|EMBL:OAI15688.1}, MKLM6_0320
GN {ECO:0000313|EMBL:ATG88600.1};
OS Methylomonas koyamae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=702114 {ECO:0000313|EMBL:OAI15688.1, ECO:0000313|Proteomes:UP000077857};
RN [1] {ECO:0000313|EMBL:OAI15688.1, ECO:0000313|Proteomes:UP000077857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-45378 {ECO:0000313|EMBL:OAI15688.1,
RC ECO:0000313|Proteomes:UP000077857};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAI27476.1, ECO:0000313|Proteomes:UP000077734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-49807 {ECO:0000313|EMBL:OAI27476.1,
RC ECO:0000313|Proteomes:UP000077734};
RA Heylen K., De Vos P., Vekeman B.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATG88600.1, ECO:0000313|Proteomes:UP000242123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM6 {ECO:0000313|EMBL:ATG88600.1,
RC ECO:0000313|Proteomes:UP000242123};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01014, 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}.
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; CP023669; ATG88600.1; -; Genomic_DNA.
DR EMBL; LUUJ01000080; OAI15688.1; -; Genomic_DNA.
DR EMBL; LUUL01000063; OAI27476.1; -; Genomic_DNA.
DR RefSeq; WP_064020193.1; NZ_LUUL01000063.1.
DR KEGG; mko:MKLM6_0320; -.
DR OrthoDB; 9807749at2; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000077734; Unassembled WGS sequence.
DR Proteomes; UP000077857; Unassembled WGS sequence.
DR Proteomes; UP000242123; 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}.
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 247 AA; 26215 MW; 7F352B97D39FF16C CRC64;
MLLIPAIDLK EGKCVRLRQG RMEDDTVFSD DPVAVAGRWV EAGAKRLHLV DLDGAFAGKP
KNADVIHAIV EAYPQVPVQI GGGIRDEDTI QAYLEAGVQY VIIGTKAVSE PHFVRDVSIE
FPGHIIIGLD ARDGKVAIDG WSKLSRHDVI DMAQKFESNG VAAIIYTDIS RDGMMQGVNV
EATAKLASSV HIPVIASGGI TNLDDIRALG AVAHEGIMGA ITGRAIYEGT LDFAEGAKLA
ASFGGED
//