ID A0A220W8K3_9SPHN Unreviewed; 366 AA.
AC A0A220W8K3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=pat {ECO:0000313|EMBL:ASK89139.1};
GN Synonyms=hisC {ECO:0000256|HAMAP-Rule:MF_01023};
GN ORFNames=SPHFLASMR4Y_02397 {ECO:0000313|EMBL:ASK89139.1};
OS Sphingorhabdus sp. SMR4y.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=2584094 {ECO:0000313|EMBL:ASK89139.1, ECO:0000313|Proteomes:UP000198359};
RN [1] {ECO:0000313|EMBL:ASK89139.1, ECO:0000313|Proteomes:UP000198359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMR4y {ECO:0000313|EMBL:ASK89139.1,
RC ECO:0000313|Proteomes:UP000198359};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Sphingorhabdus flavimaris Strain SMR4y Isolated from a
RT culture of the Diatom Skeletonema marinoi.";
RL Submitted (JUL-2017) 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;
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}.
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DR EMBL; CP022336; ASK89139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220W8K3; -.
DR KEGG; sfla:SPHFLASMR4Y_02397; -.
DR OrthoDB; 9809616at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000198359; Chromosome.
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:UP000198359};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:ASK89139.1}.
FT DOMAIN 28..358
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 366 AA; 39196 MW; 5D2AAC753DC0D4EE CRC64;
MSGPKAKDWI MGIAPYVPGK STGADGRKIV KLSANENPLG CSPAATEALN AASTSVDRYP
DPGSTRLREA IAAKYDLDPA RIICGTGSDD VLHLAANAFS GPGDEIIYVK YGFAVYDIAA
RRYGGTPVVA DDKDYGTDVD AILAKVTDRT KVIFIANPNN PTGTFTPRAE IARLHVALPG
HVLLVLDAAY AEYMDEGQDD GAMELASSQT NVLVTRTFSK IYGLAAERIG WGYAHADIIG
AMNRIRLPFN VTTAGQEAAV AALAAEDFVT MSREHNAKWR QWLSDEMSAL GNHGLKIVPS
HTNFLLVLFE GQVSAEQANA ALMDKGYAVR WLPGQGLVNG LRMTIGTEEE TRGLAQALRE
ILEAAD
//
