ID Q0FGD1_9RHOB Unreviewed; 364 AA.
AC Q0FGD1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=D-cysteine desulfhydrase {ECO:0000313|EMBL:EAU52708.1};
DE EC=4.4.1.15 {ECO:0000313|EMBL:EAU52708.1};
GN ORFNames=OM2255_04250 {ECO:0000313|EMBL:EAU52708.1};
OS Rhodobacterales bacterium HTCC2255.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52708.1, ECO:0000313|Proteomes:UP000009381};
RN [1] {ECO:0000313|EMBL:EAU52708.1, ECO:0000313|Proteomes:UP000009381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52708.1,
RC ECO:0000313|Proteomes:UP000009381};
RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000256|ARBA:ARBA00008639}.
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:EAU52708.1}.
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DR EMBL; AATR01000001; EAU52708.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0FGD1; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_1_0_5; -.
DR OrthoDB; 9801249at2; -.
DR BioCyc; RBAC367336:G1GNW-293-MONOMER; -.
DR Proteomes; UP000009381; Unassembled WGS sequence.
DR GO; GO:0019148; F:D-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005966; D-Cys_desShydrase.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01275; ACC_deam_rel; 1.
DR PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EAU52708.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR006278-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009381}.
FT DOMAIN 37..345
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 76
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 364 AA; 38806 MW; 9C1DA1857B4146DD CRC64;
MTNATQTNEV EMPFSPEMEQ SLCKDLSLTL AKFPKVRLGH LPTPLEPMDR LSEILGGPRL
WVKRDDCTGL SSGGNKTRKL EFLMADAQSK GADTIITQGA TQSNHARQTT AAAAKLGMEC
HILLEDRTGS NDHSYILNGN VLLDRLHGAS VSKRSGGTDM NAEMQDFAES LIEKGKNPYI
IPGGGSNAIG ALGYVNCARE LTEQASEIGL KVDALVHATG SAGTQAGLVA GLAAIQSDIH
LLGIGVRAPK DKQEQMVFDL AQKTADYLDT GIKIERDKVR AICDYVGAGY GLPTDGMIKA
VKLLAQSEGL LFDPVYSGKG LDGLIDQIKK GYFAGMDNVV FLHTGGSAAL FGYPETFELP
GYAN
//
