ID A0A0P1E9M7_9RHOB Unreviewed; 1070 AA.
AC A0A0P1E9M7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=3-chloro-4-hydroxyphenylacetate reductive dehalogenase {ECO:0000313|EMBL:CUH45391.1};
DE EC=3.8.1.- {ECO:0000313|EMBL:CUH45391.1};
GN Name=cprA {ECO:0000313|EMBL:CUH45391.1};
GN ORFNames=RUM4293_04304 {ECO:0000313|EMBL:CUH45391.1};
OS Ruegeria atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=81569 {ECO:0000313|EMBL:CUH45391.1, ECO:0000313|Proteomes:UP000050786};
RN [1] {ECO:0000313|EMBL:CUH45391.1, ECO:0000313|Proteomes:UP000050786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4293 {ECO:0000313|EMBL:CUH45391.1,
RC ECO:0000313|Proteomes:UP000050786};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYPS01000067; CUH45391.1; -; Genomic_DNA.
DR RefSeq; WP_058275319.1; NZ_CYPS01000067.1.
DR AlphaFoldDB; A0A0P1E9M7; -.
DR Proteomes; UP000050786; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR012832; RDH.
DR InterPro; IPR028894; RDH_dom.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR02486; RDH; 1.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF13486; Dehalogenase; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF13484; Fer4_16; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:CUH45391.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 549..579
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 754..856
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 983..1070
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 1070 AA; 117560 MW; 0F823C5A836C2FD3 CRC64;
MGIRFFSDKN RPVHMGPYPL ERLARQSVEP DLSAVPPMPV LSFHRPDQPE SIVNAMGEFQ
AMMDAIRDGF VNAVPSEIPA DPTARAHHLK AFGYFNDASM MGCGPLPAEA MLPQPCHNPD
IDRLAHALKT RQTKTLASGI DVIMADLKES MEAAPKPMDT HRHAIVFVYE HNRDPNPDEP
GSDWIMDAQD NRSCLLATEN AVVIANYIRL LGFDARAHTA MSSEVDLGKL AVTAGLASVE
NGDVVVPWLG TRFGLAAVTT EMEIAHDRPL QSMAQQPWFR TQGPAWWLGT GFAKNALNRD
AYAKRRYVDG AQPFEKLKRV EDPTTYIDEE NVARVPKRAD MFARAQFGDM GKPLQDAARG
GHYVRKAAPS FAQRRSLGAF VLLQDGDSAD GPRPTDAARN AANIKAATYF IGGDAVGLSR
CPEWAWYSHD ATGEEINPTH DQAISMIIDQ GYETMEGSSG DDWIAVAQSM RAYLRFSLLG
GVIAQQIRNL GYKAKAHTVM DGEVLQPPLL LLSGLGEVSR IGEVILNPYL GPRLKSGAVT
TDMPMEHDKP IDFGLQTFCE SCNKCARECP SGAITAGPKL MFNGYEIWKS DSQKCATYRV
TTPGGAMCGR CMKTCPWNLE GIFKERPFRW AAMNIPKAAP ALAKLDDAVG NGGLNDTKKW
WWDIELQADG AYRPTKHPLN RRDLQTDLDL QFEDQTLAVY PAYLAPHPWP YPFAMDREAG
IAAYQAMVSA EEYKNLKAAG DTSIVHRYSI AGDAPVMRVA LTKVDKMTAD VTKYEFSALN
GAPLPDWTAG AHLDVLVAPE FLRQYSMSGD PSDGSVYQIG VLREDEGRGG SALLHRIFSE
GRKVFISKPI NHFELDETAT KTFLMGGGIG ITPMIAFAHR LHALGKPFAL HYSASTRAGA
GYLNDLAAMP WADHVHFHFS DEGTRADLDA VLAGYQEGWH VYTCGPDRYM DGVIQAADRQ
GFPEEARHLE YFSVPEQPEY ENHSFTLKLA KSGRELTVPE CKDAAQVLNE AGIHVDVKCA
DGICGVCKCG VVSGDIEHRD FVLSNKQREG AIILCQSRAA EPDGVIELDL
//
