ID F5REK3_METUF Unreviewed; 365 AA.
AC F5REK3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=METUNv1_02725 {ECO:0000313|EMBL:EGK71334.1};
OS Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK71334.1, ECO:0000313|Proteomes:UP000005019};
RN [1] {ECO:0000313|EMBL:EGK71334.1, ECO:0000313|Proteomes:UP000005019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5
RC {ECO:0000313|Proteomes:UP000005019};
RX PubMed=21725020; DOI=10.1128/JB.05331-11;
RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT representative of the order Rhodocyclales.";
RL J. Bacteriol. 193:4541-4542(2011).
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:EGK71334.1}.
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DR EMBL; AFHG01000052; EGK71334.1; -; Genomic_DNA.
DR RefSeq; WP_008062608.1; NZ_AFHG01000052.1.
DR AlphaFoldDB; F5REK3; -.
DR STRING; 1000565.METUNv1_02725; -.
DR eggNOG; COG0079; Bacteria.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000005019; 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 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|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01023}; Reference proteome {ECO:0000313|Proteomes:UP000005019};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:EGK71334.1}.
FT DOMAIN 37..359
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 228
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 365 AA; 39006 MW; 58FDF83E477E9DBE CRC64;
MSVFDSAAAH IRSISPYQPG KPISELAREM GLEEAGIVKL ASNENPLGMS ERAKAAALAA
ITEVPRYPDG NGFELKQAVS RHHDLGMNQI VLGNGSNDVL EMVARALLGP GRSAVYSKHA
FAVYPLATLA AGATGIEVPA RDFGCDLDAM RAAIRDDTRV VFIANPNNPT GTFIEAGPLE
RFIASVPQDV LVVLDEAYSE YLPAALAYDS ARWLARYPNL LVSRTFSKAY GLAGLRVGYG
IGQPDVIDLL NRVRQPFNVT NVGLAAAVAA LADQDFVRRS AELNAAGLKQ LSAFFDGAGI
GYIRSYANFI AFRAGDGAGV NQRLLQQGVI VRPIAGYAMP EWLRVSVGLE SENARFIDAL
QKALA
//
