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Entry: A0A147E976_9MICC
LinkDB: A0A147E976_9MICC
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ID   A0A147E976_9MICC        Unreviewed;       246 AA.
AC   A0A147E976;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=priA {ECO:0000313|EMBL:QQC59886.1};
GN   Synonyms=hisA {ECO:0000256|HAMAP-Rule:MF_01014};
GN   ORFNames=AN277_0208915 {ECO:0000313|EMBL:OAX51397.1}, BK826_09170
GN   {ECO:0000313|EMBL:OIJ35091.1}, I6H58_02655
GN   {ECO:0000313|EMBL:QQC59886.1};
OS   Rothia kristinae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=37923 {ECO:0000313|EMBL:OAX51397.1, ECO:0000313|Proteomes:UP000053171};
RN   [1] {ECO:0000313|EMBL:OAX51397.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RUTW2-3 {ECO:0000313|EMBL:OAX51397.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA   Waterworth S., Matcher G.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OAX51397.1, ECO:0000313|Proteomes:UP000053171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171}, and RUTW2-3
RC   {ECO:0000313|EMBL:OAX51397.1};
RA   Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T.,
RA   Dorrington R.A.;
RT   "Identification of putative biosynthetic pathways for the production of
RT   bioactive secondary metabolites by the marine actinomycete Kocuria
RT   kristinae RUTW2-3.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:OIJ35091.1, ECO:0000313|Proteomes:UP000179540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCT-H5 {ECO:0000313|EMBL:OIJ35091.1,
RC   ECO:0000313|Proteomes:UP000179540};
RA   Huang B.;
RT   "Draft genome sequence of strain LCT isolated from the Shenzhou X
RT   spacecraft of China.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QQC59886.1, ECO:0000313|Proteomes:UP000595221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_1001 {ECO:0000313|EMBL:QQC59886.1,
RC   ECO:0000313|Proteomes:UP000595221};
RA   Sproer C., Gronow S., Severitt S., Schroder I., Tallon L., Sadzewicz L.,
RA   Zhao X., Boylan J., Ott S., Bowen H., Vavikolanu K., Mehta A.,
RA   Aluvathingal J., Nadendla S., Lowell S., Myers T., Yan Y., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (DEC-2020) 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}.
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DR   EMBL; LJBJ02000020; OAX51397.1; -; Genomic_DNA.
DR   EMBL; MODZ01000012; OIJ35091.1; -; Genomic_DNA.
DR   EMBL; CP066078; QQC59886.1; -; Genomic_DNA.
DR   RefSeq; WP_058730801.1; NZ_MODZ01000012.1.
DR   AlphaFoldDB; A0A147E976; -.
DR   PATRIC; fig|37923.10.peg.535; -.
DR   OrthoDB; 9807749at2; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000053171; Unassembled WGS sequence.
DR   Proteomes; UP000179540; Unassembled WGS sequence.
DR   Proteomes; UP000595221; 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:UP000053171}.
FT   ACT_SITE        13
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   246 AA;  26130 MW;  B4D159A37708B978 CRC64;
     MSTPRLQLLP AVDVAGGQAV RLVQGEAGTE TGYGDPVEAA LAWQEAGAEW VHLVDLDAAF
     GRGENTEVLR RVAERVRLKI ELSGGIRDDA SLRRALSLEP ARINLGTAAL EDPEWTRRVI
     AEHGERIAVG LDVRGTTLAA RGWTEEGGDL WEVLDRLNAD GCARYVVTDV TKDGTLRGPN
     TELLAEVARR TDRPVVASGG ISGLADLEAL RAMVPHGVEG AIVGKALYAG RFTLAEALDA
     AGRPEA
//
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