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Database: UniProt
Entry: Q1YGA8_AURMS
LinkDB: Q1YGA8_AURMS
Original site: Q1YGA8_AURMS 
ID   Q1YGA8_AURMS            Unreviewed;       368 AA.
AC   Q1YGA8;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   13-SEP-2023, entry version 82.
DE   RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000256|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000256|HAMAP-Rule:MF_01023};
GN   ORFNames=SI859A1_02918 {ECO:0000313|EMBL:EAS49317.1};
OS   Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Aurantimonadaceae; Aurantimonas.
OX   NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS49317.1, ECO:0000313|Proteomes:UP000000321};
RN   [1] {ECO:0000313|EMBL:EAS49317.1, ECO:0000313|Proteomes:UP000000321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS49317.1,
RC   ECO:0000313|Proteomes:UP000000321};
RX   PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA   Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA   McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT   "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT   Aurantimonas sp. strain SI85-9A1.";
RL   Appl. Environ. Microbiol. 74:2646-2658(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC         oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC         ChEBI:CHEBI:57980; EC=2.6.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00001045, ECO:0000256|HAMAP-
CC         Rule:MF_01023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01023};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000256|ARBA:ARBA00005011, ECO:0000256|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000256|ARBA:ARBA00007970, ECO:0000256|HAMAP-
CC       Rule:MF_01023}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAS49317.1}.
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DR   EMBL; AAPJ01000005; EAS49317.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YGA8; -.
DR   HOGENOM; CLU_017584_3_3_5; -.
DR   BioCyc; AURANTIMONAS:SI859A1_02918-MONOMER; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000321; Unassembled WGS sequence.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01141; hisC; 1.
DR   PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_01023}; Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000321};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:EAS49317.1}.
FT   DOMAIN          33..359
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         222
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   368 AA;  38946 MW;  B4E4B7CF63E82697 CRC64;
     MRTMRPVPTK GVLDIEAYVP GKSKAPAGVT LHKLSSNETP LGPPPAAREA AAAALTQLEV
     YPDGQSSALK DAIAEVHGLD GRHILCGNGS DELLGLLCQC YLAPGDEAIH TEHGFLVYRI
     QILARGATPV AVKETDATAD VDAILAAVTG KTKLVFLANP NNPTGTYLPF DEVRRLHAGL
     PGHVILVLDA AYAEYVRRND YGAGIELVSS SENVVMTRTF SKIYGLAGLR IGWMYGPEAI
     VDALDRVRGP FNLNAAAIAA GAAAIRERAF IESAIDHNTR WLEWTTGALE GLGLTVTPSV
     GNFVLVHFPD APGRTAADAD AFLTSKGFIL RRVAGYGFPN ALRMTIGTEE ANRGAVAALA
     DFLGRGQP
//
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