ID B8FFK3_DESAL Unreviewed; 549 AA.
AC B8FFK3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ACL04263.1};
GN OrderedLocusNames=Dalk_2570 {ECO:0000313|EMBL:ACL04263.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL04263.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL04263.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL04263.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP001322; ACL04263.1; -; Genomic_DNA.
DR RefSeq; WP_015947336.1; NC_011768.1.
DR AlphaFoldDB; B8FFK3; -.
DR KEGG; dal:Dalk_2570; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_7; -.
DR Proteomes; UP000000739; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR022517; Asp_decarboxylase_pyridox.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000000739}.
FT MOD_RES 347
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 549 AA; 61050 MW; 510C1A3169E1F287 CRC64;
MDRTSEAQRR ELVANRETLK RIFIMREDDS AKATLLKYME QIFFGLQDFL KDHVGITEER
SLREMASRFQ NSLISEQPEK KLADVITELV EDIAPHAVNV ASPYFVGHMT SAMPFFMVHL
AAFVAALNQN VVKLETSKIV SIVEKQLLAK IHRMIYQQDD AFYSRHIQSV DTSLGGFTED
GTLANMTALW VARNSILNQA EGFAGVEQEG MFAAYQALGI ERMVVLVSQL GHYSLRKAAG
LLGLGNKNVI GLPIDANNRV DVDALARAVK EISADPKTRI MAVVGIAGAT ETGSVDPLPR
IAEICAEHNI HFHADAAWGG PTLFSEKYKH LLEGIDMADS VTIDGHKQFY MPMTCGMVYF
KNPWAMDAIA YHSTYIARPG SVDLGIKSLA GSRASTSLIL DSALKVMGVK GYGILVEHGI
GLARQFAKEI RARENFELVT PPELNILTYR YVPARLQERL QNAEPKEAVR INQCLNALNI
VLQRDQREAG KSFVSRTTFR RPPEKGGDVV VLRTVLMNPM TRLRILKEIL DEQEQICQTK
LGKAFGAIC
//
