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Database: UniProt
Entry: M7MH88_9FLAO
LinkDB: M7MH88_9FLAO
Original site: M7MH88_9FLAO 
ID   M7MH88_9FLAO            Unreviewed;       395 AA.
AC   M7MH88;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=D778_02451 {ECO:0000313|EMBL:EMQ95617.1};
OS   Xanthomarina gelatinilytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Xanthomarina.
OX   NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ95617.1, ECO:0000313|Proteomes:UP000012024};
RN   [1] {ECO:0000313|EMBL:EMQ95617.1, ECO:0000313|Proteomes:UP000012024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK20 {ECO:0000313|EMBL:EMQ95617.1,
RC   ECO:0000313|Proteomes:UP000012024};
RA   Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Formosa sp. AK20.";
RL   Submitted (DEC-2012) 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}.
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:EMQ95617.1}.
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DR   EMBL; ANLA01000005; EMQ95617.1; -; Genomic_DNA.
DR   RefSeq; WP_007648362.1; NZ_ANLA01000005.1.
DR   STRING; 1137281.D778_02451; -.
DR   PATRIC; fig|1137281.3.peg.1040; -.
DR   eggNOG; COG0436; Bacteria.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000012024; Unassembled WGS sequence.
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   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:EMQ95617.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012024};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EMQ95617.1}.
FT   DOMAIN          31..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   395 AA;  43682 MW;  35B4A28902A0FDC0 CRC64;
     MSLLSERVLN MSTSATLAMA AKTRELKAQG KDIIGLSLGE PDFNTPDYIK EAAIQAINEN
     YNSYSPVDGY VELKEAIITK FKRDNNLSYT LPQIVVSTGA KQALANVASV MINKGDEVIL
     PCPYWVSYAD IVELFEGVPV EVKTTIDTDF KMTPEQLEAA ITPKTKMIWY SSPCNPSGSL
     YSTEELRALA DVLQKHPDIY VVSDEIYEHI NFTTDGHASM AQFEDMFDRT ITVNGVSKAF
     AMTGWRIGYI GAPEVIARAC NKMQGQITSG ANCIAQRATI TALNEPPSKV KYMIDEFKIR
     RDLVLDLLSE IEGFKTNTPE GAFYVFPNIS YYFGKTLRGK TIHNATDFSL YLLEEALVAT
     VTGDAFGNPD CIRISYAASQ AQIIEAIKRI KEAVS
//
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