ID A2SS57_METLZ Unreviewed; 369 AA.
AC A2SS57;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABN07163.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ABN07163.1};
GN OrderedLocusNames=Mlab_0994 {ECO:0000313|EMBL:ABN07163.1};
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358 {ECO:0000313|EMBL:ABN07163.1, ECO:0000313|Proteomes:UP000000365};
RN [1] {ECO:0000313|EMBL:ABN07163.1, ECO:0000313|Proteomes:UP000000365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z {ECO:0000313|Proteomes:UP000000365};
RX PubMed=21304657; DOI=10.4056.sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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DR EMBL; CP000559; ABN07163.1; -; Genomic_DNA.
DR RefSeq; WP_011833366.1; NC_008942.1.
DR AlphaFoldDB; A2SS57; -.
DR STRING; 410358.Mlab_0994; -.
DR GeneID; 4794640; -.
DR KEGG; mla:Mlab_0994; -.
DR eggNOG; arCOG01130; Archaea.
DR HOGENOM; CLU_017584_4_3_2; -.
DR OrthoDB; 372018at2157; -.
DR Proteomes; UP000000365; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
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 PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF3; ASPARTATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000313|EMBL:ABN07163.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Reference proteome {ECO:0000313|Proteomes:UP000000365};
KW Transferase {ECO:0000313|EMBL:ABN07163.1}.
FT DOMAIN 28..364
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 369 AA; 39290 MW; D9EFBA9F4259F1B1 CRC64;
MTDFASRVTS IDISGIRKMF ESAAPGSINM GLGQPDFDTP ENIKNAAFKA IAEGKTGYTN
NAGIDELRAA IAAKLKTENG LSYQPADILI TAGGSGALHA AIFSLVENGQ KVVFNNPGFV
SYGSLATLAG GIPDPVALKP DLHLDIEALK EHFSDKNTKV MVLNSPANPT GAVETKETIK
AVVESAADYG VTVLSDEVYE KFCYGDTEFV SAARFGENVV TINAASKTYA MTGWRIGFMA
ASREIIDQAV KIQQYSLACP TSIAQYAALE AYTGDQSSIG VMKKEYEARR NLLIGGLREM
GISVEMPEGA FYAFPKLDLD TVMKIVEAGV IITPGAAFGS KGVGYARMSY ATSQENIKIA
LDRIRTVVA
//
