ID A0A0F5AME2_9GAMM Unreviewed; 555 AA.
AC A0A0F5AME2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Cytochrome D ubiquinol oxidase subunit II {ECO:0000313|EMBL:KKA43822.1};
GN ORFNames=WN56_16090 {ECO:0000313|EMBL:KKA43822.1};
OS Salinivibrio sp. KP-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Salinivibrio.
OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA43822.1, ECO:0000313|Proteomes:UP000033449};
RN [1] {ECO:0000313|EMBL:KKA43822.1, ECO:0000313|Proteomes:UP000033449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA43822.1,
RC ECO:0000313|Proteomes:UP000033449};
RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA Kaur N., Bala M., Mayilraj S.;
RT "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT nov., a novel halotolerant gammaproteobacterium isolated from marine
RT sediment and emended description of the genus Salinivibrio.";
RL Submitted (MAR-2015) 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|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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:KKA43822.1}.
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DR EMBL; LAQR01000048; KKA43822.1; -; Genomic_DNA.
DR RefSeq; WP_046075922.1; NZ_LAQR01000048.1.
DR AlphaFoldDB; A0A0F5AME2; -.
DR PATRIC; fig|1406902.3.peg.3233; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000033449; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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; 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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000033449}.
FT MOD_RES 342
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 555 AA; 62393 MW; 9BDFBE3C32612D0F CRC64;
MSCSLPTHAL TATFTQQYQT IRQHFFNRDP DRWPVYRTPE LAHWLENGMH PAVADAAHPF
SQQTHIPEQS DISAKTLPNL ALQAATYSKD WTSPRAVENV ITAPCDPAIH GALLATMANP
NLVYSEYAGM SVELEKTLVR QVANLIGYDP DQATGIFTQG GTFGNLYGYL MGLRKQFPLS
GQRGFQGQDF RMINSLAGHY SNMTNLGLLG TDIPNQVLRI KVDANNRLDL DDFAYSLNHC
LAEKMPVPTI LLTFGTTDTF AIDDIERIYQ ITTRACERFN TSVRPHIHVD AAVGWPLVMF
NDYDFAANPI GINAATRNKL QALIPRIRGL RFADSITIDF QKWGFVPYTA SLVMFKQKTD
MEHLKQDPHY FSYFETSKTQ QTHLQSTIEC SRGAAGAYGS YCALNMLGKR GYQTMIAHSL
QNAEYLKAHL DALPHCKIVA GDNLGPTVAF RLYQPSPTLD VNVMFQQEQT LHQVGARIDS
ITQHSLFHRQ HFLARQGKTL QTNWVESIAH TEFDPNGQCL FIPGEKAVFL NPYTRYTHID
EFVASLCPEH AEQLV
//
