ID A0A0X8D4A7_9BACL Unreviewed; 392 AA.
AC A0A0X8D4A7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=ACH33_12135 {ECO:0000313|EMBL:AMA73529.1};
OS Aneurinibacillus sp. XH2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA73529.1, ECO:0000313|Proteomes:UP000065566};
RN [1] {ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA Xi L.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMA73529.1, ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA73529.1,
RC ECO:0000313|Proteomes:UP000065566};
RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT China.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP014140; AMA73529.1; -; Genomic_DNA.
DR RefSeq; WP_057899256.1; NZ_CP014140.1.
DR AlphaFoldDB; A0A0X8D4A7; -.
DR STRING; 1450761.ACH33_12135; -.
DR KEGG; anx:ACH33_12135; -.
DR Proteomes; UP000065566; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:AMA73529.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000065566};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AMA73529.1}.
FT DOMAIN 31..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 392 AA; 43132 MW; 9E2A900A09ED4874 CRC64;
MKVAKRVAQI TPSKTLAITA KAKELRSQGY DVVGLGAGEP DFNTPKHIID AAVQAMEEGQ
TKYTAAAGIP ELKKAICEKL KRDNHLTYKP SQIVVCNGAK HALYNLFQAI VDPGDEVIVP
IPYWVSYPEM ITLADGVPVF VEGKEENEFK ITPEQLRQAI TDKTRAVILN SPSNPTGSVY
AREELEALAQ VCIEKKILIV SDEIYEKLIY DGEEHVSIAS LSPEAYELTI VINGMSKPYS
MTGWRIGYAA GNEEIIKAMA NLSSHSTSNP TTFAQYGALA ALTGTQEPLE MMKAEFDKRR
KAVVKLMNEI DGIHCVEPKG AFYLFANVSE AMRKGGYNDV DEWAQALLEK EYVALIPGSG
FGAPNHIRIS YATSLEQLEK GIARIKKFVE GR
//
