ID A0A0M1JHD4_9GAMM Unreviewed; 391 AA.
AC A0A0M1JHD4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=TI05_09100 {ECO:0000313|EMBL:KOR32150.1};
OS Achromatium sp. WMS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604836 {ECO:0000313|EMBL:KOR32150.1, ECO:0000313|Proteomes:UP000036918};
RN [1] {ECO:0000313|EMBL:KOR32150.1, ECO:0000313|Proteomes:UP000036918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS3 {ECO:0000313|EMBL:KOR32150.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
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}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:KOR32150.1}.
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DR EMBL; JXSO01000178; KOR32150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JHD4; -.
DR PATRIC; fig|1604836.3.peg.1093; -.
DR Proteomes; UP000036918; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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 PANTHER; PTHR43643:SF6; 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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000036918}.
FT DOMAIN 43..386
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 391 AA; 44604 MW; EEB7F76D13DB371A CRC64;
MPIARLNIAT KKAFSRQIRG YTDSEKTAHD RVCEIVAECN IKEILRFDLG QNPNGCAPEV
AEKLQYLSEQ NDAHLILKNY PGTEISNLRD KLANMHGISP DQLLFSAGTE QMIGLIARSI
LEEKDSILVN RPSFFVFENV SNKMGAHILH LDLNVESGFN WTEQTLERFK VMQKQYIPKI
IWIANPNNPT GQAIADDILE EILRFTANYP TLVVIDEAYG EYLDPPNGFK SISQIVPNQR
NLLVLRTFSK AYGLASIRLG YAITSDENLS AAIRLHSNAY PVSELSIMLA NFALNHMDYL
EQTRQETIRC RKQFLEWTKS IPKLEVINSD CSILMLKHKH YDSITLRRLL EKLGIFTSSI
PGSDEIAKSF IRISLGRERE NRILYEQLRC I
//
