ID G0L6L0_ZOBGA Unreviewed; 395 AA.
AC G0L6L0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Histidinol-phosphate aminotransferase {ECO:0000313|EMBL:CAZ97017.1};
GN Name=hisC2 {ECO:0000313|EMBL:CAZ97017.1};
GN OrderedLocusNames=zobellia_2870 {ECO:0000313|EMBL:CAZ97017.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ97017.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ97017.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; FP476056; CAZ97017.1; -; Genomic_DNA.
DR RefSeq; WP_013994212.1; NZ_JAUOSS010000012.1.
DR AlphaFoldDB; G0L6L0; -.
DR STRING; 63186.ZOBELLIA_2870; -.
DR KEGG; zga:ZOBELLIA_2870; -.
DR PATRIC; fig|63186.3.peg.2819; -.
DR HOGENOM; CLU_017584_3_3_10; -.
DR OrthoDB; 9813612at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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 InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR006311; TAT_signal.
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; PS51318; TAT; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:CAZ97017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:CAZ97017.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..395
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003402465"
FT DOMAIN 67..387
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 395 AA; 43527 MW; 1FDB6A19B8FF0DDC CRC64;
MKTLDRRAWL KRGALTAAGA IAAPYLSYGA FGNEPVTIDA QGNLPYTPFF KEYLPYEVDK
PVELLAKLNA NENPYGPSPM AVDAMQKYAP KGNRYAWKEL YTLIDKIAVL EGVEAETIMM
GPGSSDLLEK TAMVFFQNGG NIVSADPSYM SLIKVAEATG ATWKPIKLKD DWSHDLPAME
AAIDADTKLV YICNPNNPTG SMTDHEELID FCSRVSEKVP IFVDEAYLGF LDDAAKKSMV
SLINEGKNVM IARTFSKIQG MAGLRVGYMV AQPETLAIIQ KITRGGMGIS LPSVYAAMAS
MDDIEFSNKT RKLNSECREY VYSVLDGMGY SYVPSSTSFI IFPIEMEGKA FLEKMTAEGV
GVRAFSIMDK NWCRVSMGTM EEMKLFTTAL QKVLA
//
