ID A0A222FGB2_9GAMM Unreviewed; 377 AA.
AC A0A222FGB2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:ASP37672.1};
GN ORFNames=CHH28_02855 {ECO:0000313|EMBL:ASP37672.1};
OS Bacterioplanes sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bacterioplanes.
OX NCBI_TaxID=1249553 {ECO:0000313|EMBL:ASP37672.1, ECO:0000313|Proteomes:UP000202440};
RN [1] {ECO:0000313|EMBL:ASP37672.1, ECO:0000313|Proteomes:UP000202440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NV9 {ECO:0000313|EMBL:ASP37672.1,
RC ECO:0000313|Proteomes:UP000202440};
RA Rehman Z.U.;
RT "Annotated genome sequence of Bacterioplanes sanyensis isolated from Red
RT Sea.";
RL Submitted (JUL-2017) 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:PIRSR600183-50};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|RuleBase:RU003737}.
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DR EMBL; CP022530; ASP37672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222FGB2; -.
DR KEGG; bsan:CHH28_02855; -.
DR OrthoDB; 9802147at2; -.
DR Proteomes; UP000202440; Chromosome.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProt.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000202440}.
FT DOMAIN 29..259
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 260..354
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 50
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 377 AA; 41800 MW; 95BCB4C39C3E159C CRC64;
MQSIERLKPM LQEEPCALST PCYVYSVSAV ERNFKALKQA LGTQLIYSFK ANSNLELMVR
CGHIFTDGIE LASQGELGLM ATGKAPRYIN NPSADKNFLR AAIASKAQII IDHPAQLEVM
KDFVGKRPIA PLILRLNPCV LSDYDPQPSL RANHFGMDWP LLQQAINRCQ QLQLEVGGVH
LFTGSYQFER HAISTAQAAL QCVERIQQLL DGPLNFLNLG GGFDEHWQQN DFDFEQYRHL
LAEFPSHVTL AHESGRGIMA SAGHFVTKVR YTKTIEDRHY AICDGGMAQN FLLAQTENTF
RRYAQPTVVH NTTPAGHTGT WLLAGTSCNK DDLIGQLNDA SIGVGDFAIF ADCGAYNASY
TVSPFLNLPT ANTYIVE
//
