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Database: UniProt
Entry: M1PT24_DESSD
LinkDB: M1PT24_DESSD
Original site: M1PT24_DESSD 
ID   M1PT24_DESSD            Unreviewed;       400 AA.
AC   M1PT24;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Putative PLP-dependent enzyme possibly involved in cell wall biogenesis {ECO:0000313|EMBL:AGF79461.1};
GN   OrderedLocusNames=UWK_02931 {ECO:0000313|EMBL:AGF79461.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79461.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP003985; AGF79461.1; -; Genomic_DNA.
DR   RefSeq; WP_015405147.1; NC_020304.1.
DR   AlphaFoldDB; M1PT24; -.
DR   STRING; 1167006.UWK_02931; -.
DR   KEGG; dsf:UWK_02931; -.
DR   PATRIC; fig|1167006.5.peg.3168; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_7_2_7; -.
DR   OrthoDB; 9771070at2; -.
DR   Proteomes; UP000011721; Chromosome.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         186
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   400 AA;  43746 MW;  DBEC3A25CF81E2F1 CRC64;
     MPGFEVFGDE EKRQISDVLD TGVLFRYEFG EQRKNVYKVL EFEKNFASYC GAGFAQAVTS
     GTAALKVALA ALGVGPGDEV ITQGFTFVAT WEAILDIGAI PVFTEIDETL NMDPEDLKTK
     INDKTRCIIP VHMLGAMARI EEIVAIASKH NIPVLEDTAQ AAGGTIKGQH LGTFGNCGTF
     SFDSVKTMTT GEGGMIITND EEMWRTMSEY HDHGHDHVVN PGGRGGEGRR FVGFNYRMME
     LQGAMGIAQL AKLDSMIAAQ KNHKAKLRQA ASAIPGVQFR SLVDEEGDTA TFFAFIMESS
     EQCQRINAIL KESGVGAINF SENSWHFYPS WEHLMKGSTI TASGWPFAEP GGKRRVVYDP
     NLLPQSADIM SRTLVYPVSV KMSDEQLKKM CDALGRAATA
//
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