ID A0A1T5NZY0_9BACT Unreviewed; 381 AA.
AC A0A1T5NZY0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05660461_3287 {ECO:0000313|EMBL:SKD06051.1};
OS Chitinophaga ginsengisegetis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD06051.1, ECO:0000313|Proteomes:UP000190166};
RN [1] {ECO:0000313|EMBL:SKD06051.1, ECO:0000313|Proteomes:UP000190166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD06051.1,
RC ECO:0000313|Proteomes:UP000190166};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUZZ01000002; SKD06051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5NZY0; -.
DR STRING; 393003.SAMN05660461_3287; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000190166; Unassembled WGS sequence.
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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04732; HisA; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01014; HisA; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000182; GNAT_dom.
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; PF13673; Acetyltransf_10; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS51186; GNAT; 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:UP000190166}.
FT DOMAIN 1..135
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT ACT_SITE 273
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ SEQUENCE 381 AA; 41741 MW; 715376E6839EBD1D CRC64;
MNIRKISADD TLQLRRDVLY PNESLDAVKV DHDVDGLHFG VFDQGQLVTV VSLFLGRDSA
QFRKLATAQA AQGKGFGEAI LAHLADICKK EKIKLLWCNA RDTAVTFYDR LGYTTKGDYF
IKGGITFVRM ELPLDQQNMT TKKFEIIPAI DIIGGKCVRL TQGDYNQQKV YNEHPLEVAK
EFEAIGVRRL HLVDLDGAKK GAVVNWKVLE SIAGKTSLVT DFGGGIKTDK DLEIVFQSGA
ALATIGSVAV KQPELFFSWV KQYGADKIFL GADVKEEKIA VGGWLETTEL SVFDFLESNI
ARGVTNIFCT DIAKDGLLQG PSIDLYKKII ERFPGINFVA SGGVSNIEDV AALQEIGCSG
AIIGKAIYEG NISMDALKTF L
//
