ID   A0A0E3S0X8_METMZ        Unreviewed;       475 AA.
AC   A0A0E3S0X8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AKB72522.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AKB72522.1};
GN   ORFNames=MSMAC_2632 {ECO:0000313|EMBL:AKB72522.1};
OS   Methanosarcina mazei C16.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434113 {ECO:0000313|EMBL:AKB72522.1, ECO:0000313|Proteomes:UP000033071};
RN   [1] {ECO:0000313|EMBL:AKB72522.1, ECO:0000313|Proteomes:UP000033071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C16 {ECO:0000313|EMBL:AKB72522.1,
RC   ECO:0000313|Proteomes:UP000033071};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP009514; AKB72522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3S0X8; -.
DR   KEGG; mmac:MSMAC_2632; -.
DR   PATRIC; fig|1434113.4.peg.3297; -.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   Proteomes; UP000033071; Chromosome.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AKB72522.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AKB72522.1}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  52928 MW;  E3E196F5C97D001B CRC64;
     MEGERFLNHR TPEELEKWKN TGKTEGSEDS MKELETEFNS FEQEVGLLDT VGPKAREIIG
     QDCNMVSACV SRPYPLVVDR AKGSVVRDID GKEYIDFVAG IAVMNAGYSN PEVQAAISAQ
     LEKMVHCGYG DFFAEPPLKL AKKLRDLSGY SKVFYCNSGA ESIEAAMKLS LWKTKRQNFI
     SFYNAFHGRT LGALSLTCSK VRHKEHFPTI RTVHTDYAYC YRCPLNLDYP SCGIECAKQI
     ENLVFRRELS PEDTAAVFVE PIQGEGGYIV PPVEFHKEVR RICTDNDVLL VADEVQTGCF
     RTGPFLAMEN FEVRADITCL AKALGSGLPI GAMLADNELM DWPPGVHSNT FGGNLLSSAA
     ALASLEFLEK ENTENHVREM GAHIRHRLRE LQENFPCIGD VRGLGLMTGV EIVKPDKSID
     PVRRDKIIRE AFKDGVLLLP CGDSVIRFSP PLVMTDEEAD LGLDKFEKAL KKAVR
//