ID A0A261GJP6_9GAMM Unreviewed; 956 AA.
AC A0A261GJP6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=BTA51_18935 {ECO:0000313|EMBL:OZG71719.1};
OS Hahella sp. CCB-MM4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=1926491 {ECO:0000313|EMBL:OZG71719.1, ECO:0000313|Proteomes:UP000215632};
RN [1] {ECO:0000313|EMBL:OZG71719.1, ECO:0000313|Proteomes:UP000215632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM4 {ECO:0000313|EMBL:OZG71719.1,
RC ECO:0000313|Proteomes:UP000215632};
RA Sam K.-K., Lau N.-S., Dinesh B., Go F., Amirul A.-A.A.;
RT "Genome sequence of Hahella sp. CCB-MM4 and discovery of its potential
RT applications.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:OZG71719.1}.
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DR EMBL; MRYI01000012; OZG71719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261GJP6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000215632; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02754; CCG; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000215632}.
FT DOMAIN 38..265
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 529..560
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 588..617
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 686..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 104037 MW; CE5436B0E012C169 CRC64;
MTSNLTAFIQ KLATQIPSDR LIQDQLRRLA YGTDASFYRL IPQLVVRAES EAEIVHLIKS
AQEFGAPLTF RAAGTSLSGQ AVTDSILVQL QGWRQHEILE NGSRIKLQPG IIGAHANQYL
APFSRKIGPD PASINAARIG GIAANNASGM CCGTKHNSYH TLADMRLILA DGTILDTADH
NSRLTFAQTH GDVLQGLLKL RQKILSNANL EKKIRHKYRL KNTTGYGLNA LLDYDDPIDI
LTHLMIGSEG TLGFISNITY QTVEDHPCKA TTLVFFADVK TTCEAVSALK SSPVDAVELI
DRRGLSAIES KSGVPDFVKQ LPDGAAALLI ETRAADQSLL NDRKEAISQV LSGFTVINQL
PFTEVPEQIA QLWNIRKGLF PALGALRNTG TTVVIEDVAF PVADLADGVL KLQSLFDRHQ
YQDALIFGHA LEGNLHFVFA QDLNDPAAID RYRDLMEDVA HLVAVEYGGS LKAEHGTGRN
MAPFVALEWG EEAYAIMQEI KGLLDPNNIL NPGVILNSDL EVHLKNLKPM PVVDSLVDKC
IECGFCEPVC PSRNLTLTPR QRIVISREIA RLETSNEDSA SLAELQRDYL YQGDDTCAAC
GLCATSCPVG INTGDLTRLH RHRQNLPQAG KAQWAAGHFA GMTATTRVML AAADKMHQLL
GPGILGGASS TITKVSGGKV PTWHPYLPKA APRLPTSKRT PSSGSPPCQP DDLVYKAVYF
SSCATRTMGP ARGDANSQAV TQANLSLLKK AGYEVIFPES LDSLCCGMPF QSKGFFDTAN
QKAEQLLSAL WQASEYGKYP IFSDTSPCTM RLLDQVKTLP EFQQIHILDT VEFIHDHLLQ
RLEIHPMNQP TALHITCSTT KMGLAGKLTH IAKVCCTEIF IPEDITCCGF AGDKGFSRPE
LNASALLPLK AQVEEKQCES GVSNSRTCEI GLSLHSGIHY HGISLLVDAV SQPKPN
//
