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Database: UniProt
Entry: A0A292RF27_9BACT
LinkDB: A0A292RF27_9BACT
Original site: A0A292RF27_9BACT 
ID   A0A292RF27_9BACT        Unreviewed;       464 AA.
AC   A0A292RF27;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:DAA96506.1};
GN   ORFNames=CPT80_04185 {ECO:0000313|EMBL:DAA96506.1};
OS   Candidatus Gastranaerophilales bacterium HUM_9.
OC   Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales.
OX   NCBI_TaxID=1916320 {ECO:0000313|EMBL:DAA96506.1, ECO:0000313|Proteomes:UP000218540};
RN   [1] {ECO:0000313|EMBL:DAA96506.1, ECO:0000313|Proteomes:UP000218540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HUM_9 {ECO:0000313|EMBL:DAA96506.1};
RX   PubMed=28360330; DOI=.1126/science.aal3794;
RA   Soo R.M., Hemp J., Parks D.H., Fischer W.W., Hugenholtz P.;
RT   "On the origins of oxygenic photosynthesis and aerobic respiration in
RT   Cyanobacteria.";
RL   Science 355:1436-1440(2017).
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}.
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:DAA96506.1}.
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DR   EMBL; DABG01000012; DAA96506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292RF27; -.
DR   STRING; 1916320.GCA_002103075_00110; -.
DR   Proteomes; UP000218540; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
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:DAA96506.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:DAA96506.1}.
SQ   SEQUENCE   464 AA;  53068 MW;  3193F8CB518AB9B4 CRC64;
     MVCLEKNTIT DSEIKELDAV YDSYGDTVHY SPDPKVFRGC EGSYMYDSND TPYLDLQMMY
     SACNFGYRNQ RINDAILDQM NTMPQLCPKY LYDYKPMLAK KMADMNFKRF GEKGRIHFNV
     GGAQANEDAL KVIRNYTGRN AVFAFQGGYH GRTIGATCMT SSFRYREKYG HFGDRAQFIP
     FPYCFRCPYG MKCDSCNHFC VKQVAKMFES EYNSYYDPKT GECEYKAFYC EPILGTGGYI
     NPPEWYFKEL KQILDEHNIM FCVDEVQMGM FRTGKLWAIE NYGVTPDIMS FAKSITNGMN
     PLAGFWAKEK FVAPDVFTPG SAHSTYCSNP LGVRAAYEVM SIVEEDEKKL EHDIPIKSAR
     FMNGLKYLQS KYKSIGDVDG IGFALRIELT KEDGITPNRE LCDALQEEGL KGDLSYNGKK
     CGLVLNNGGF YKNIITLVPQ LYISDEEIDM AIDLFDQLFD RLDK
//
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