ID D8ISW8_HERSS Unreviewed; 265 AA.
AC D8ISW8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 ECO:0000313|EMBL:ADJ65534.1};
GN OrderedLocusNames=Hsero_4064 {ECO:0000313|EMBL:ADJ65534.1};
OS Herbaspirillum seropedicae (strain SmR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ65534.1, ECO:0000313|Proteomes:UP000000329};
RN [1] {ECO:0000313|EMBL:ADJ65534.1, ECO:0000313|Proteomes:UP000000329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ65534.1,
RC ECO:0000313|Proteomes:UP000000329};
RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA Weiss V.A., Yates M.A., Souza E.M.;
RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT fixing, plant-growth promoting beta-Proteobacteria.";
RL Submitted (APR-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|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}.
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DR EMBL; CP002039; ADJ65534.1; -; Genomic_DNA.
DR RefSeq; WP_013235993.1; NC_014323.1.
DR AlphaFoldDB; D8ISW8; -.
DR STRING; 757424.Hsero_4064; -.
DR KEGG; hse:Hsero_4064; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_4; -.
DR OrthoDB; 9807749at2; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000000329; 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:UP000000329}.
FT ACT_SITE 8
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT ACT_SITE 139
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ SEQUENCE 265 AA; 28342 MW; DEDD2C8B0559416F CRC64;
MLLIPAIDLK DGHCVRLKQG DMDQATVFSE DPAEMALHWL KQGARRLHLV DLNGAFAGKP
KNEAAVKAIL KAVASFAEEN EVEEIPVQLG GGIRDLDTIE RYLDDGLSYI IIGTAAVKNP
GFLHDACSAF PGQIIVGLDA KDGKVATDGW SKLSGHEVVD LAQKFEGYGC EAIVYTDIGR
DGMMGGVNIE ATVRLAQAVT IPIIASGGVH NVGDVEALCR VEDEGIEAVI CGRSIYEGTL
DLRSGQDRAD ELTRELEANR LSGSK
//
