HIS4_NITOC
ID HIS4_NITOC Reviewed; 249 AA.
AC Q3J6Q2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
DE EC=5.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01014};
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
GN Name=hisA {ECO:0000255|HAMAP-Rule:MF_01014}; OrderedLocusNames=Noc_3053;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_01014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01014}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC Rule:MF_01014}.
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DR EMBL; CP000127; ABA59494.1; -; Genomic_DNA.
DR RefSeq; WP_002813359.1; NC_007484.1.
DR AlphaFoldDB; Q3J6Q2; -.
DR SMR; Q3J6Q2; -.
DR STRING; 323261.Noc_3053; -.
DR EnsemblBacteria; ABA59494; ABA59494; Noc_3053.
DR KEGG; noc:Noc_3053; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_6; -.
DR OMA; EWLHLVD; -.
DR OrthoDB; 794219at2; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000006838; 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; -; 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 PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00007; TIGR00007; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase;
KW Reference proteome.
FT CHAIN 1..249
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000229064"
FT ACT_SITE 8
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ SEQUENCE 249 AA; 26661 MW; 91DB9C95C4B2DB77 CRC64;
MLLIPAIDLK GGKCVRLRQG RMEDDTVFSD DPVAVALHWA EAGAKRLHLV DLDGAFAGQP
VNADIIYHIA QALPDMDIQV GGGIRDSDTI QTYLDAGVRY AIIGTKAINA PHFVADACLE
FPGHILLGLD AREGKIAING WSKLSRHNLI DIAQRFEKDG VEAIIYTDIQ RDGMMKGVNI
EATSELAKAI NIPVIASGGV SSLTEIEALC QHEQDGIGGA IIGRALYEEK IQLAEALAIA
KRLSGESTA