ID D2BBF2_STRRD Unreviewed; 474 AA.
AC D2BBF2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Diaminobutyrate decarboxylase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Sros_1177 {ECO:0000313|EMBL:ACZ84175.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ84175.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ84175.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
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; CP001814; ACZ84175.1; -; Genomic_DNA.
DR AlphaFoldDB; D2BBF2; -.
DR STRING; 479432.Sros_1177; -.
DR KEGG; sro:Sros_1177; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_11; -.
DR Proteomes; UP000002029; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
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:UP000002029}.
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 474 AA; 51269 MW; DEEA7B333389F832 CRC64;
MAICRGFDQY PGVIWNVEEF ARAAAVTADG LAAYVDESQR GLPPVIRRRP PREVAERLGL
VRWIREGGMT PDSYAEFLAA YLDEGTRLHH PAYLGHQIAA PDFPAALADF VHGATNNPMA
VYEMGASAAT VEFEVLRWML DKVGFGETGG GVLTHGGSLA NLTALLAARA AAVPEAWTDG
VPADLALLAP ASAHYSLTRA AAILGLGERA VMPLDVDGLG RVDVARLPEA LDRVRRAGRR
PMALVASACS TGTGLYDDLR GIGEFCTANG VWFHVDGAHG ASALLAEEHR HLLDGIELAD
SLIWDAHKML RTSSLAAAVL TRREGDLDAA FRQRASYLFY GDQGFDLIGR TVECSKAELG
LKVFLNLAWR GERGLGDYVA RQYATAHRFW ELARERPGFE CPYEPESNIV CFRYGGADQA
EIRERLMADG AFQLTSAEID GVRHLRVTVM APATDDKTLE ALLDRIGGER GPGG
//
