ID A0A140L2Q0_9CLOT Unreviewed; 376 AA.
AC A0A140L2Q0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=hisC2_2 {ECO:0000313|EMBL:KXG74825.1};
GN Synonyms=hisC {ECO:0000256|HAMAP-Rule:MF_01023};
GN ORFNames=AN619_21660 {ECO:0000313|EMBL:KXG74825.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG74825.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG74825.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG74825.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; Evidence={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|HAMAP-Rule:MF_01023}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-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:KXG74825.1}.
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DR EMBL; LOEE01000046; KXG74825.1; -; Genomic_DNA.
DR RefSeq; WP_068556850.1; NZ_LOEE01000046.1.
DR AlphaFoldDB; A0A140L2Q0; -.
DR STRING; 520762.AN619_21660; -.
DR PATRIC; fig|520762.4.peg.2394; -.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000070456; 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; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR PANTHER; PTHR43643:SF3; 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:UP000070456};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:KXG74825.1}.
FT DOMAIN 32..353
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 225
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 376 AA; 42500 MW; E3051D532FC9A3DB CRC64;
MAIQHRTEIA DLQPYKPGKP IDDVKREYGL THVVKLASNE NPLGCSPKVM EAIRQALDSL
SLYPDGNCTE LKTALAAKFG LKPSQILPSG GSDEMVDMIS KAYVNPGDEV IVADITFPRY
MATAKMMGGT PVVVPLKNFT YDLDAMYHAI TDKTKLIWLC NPNNPTGTMF GEKALMEFLD
KVPQHIMVIY DEAYNEYVTR RDYPQEACRL IDKYPNIVVM RTFSKIYGLA ALRVGYTIAR
EEIITTLNKI RNPFNVNTLA QKAAIAALAD QDFIQKAYAL NKQGKEYLYQ AFDQMDISYA
PSEANHIFFN CRYDAQEIFE ELQKRGVIIR PMFATYARVS IGTMEENQLF IETLKEVFNI
LETKKEAACT CCCDCK
//
