ID A0A0S9MX05_9BURK Unreviewed; 1017 AA.
AC A0A0S9MX05;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:KQP37534.1};
GN ORFNames=ASF44_14400 {ECO:0000313|EMBL:KQP37534.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP37534.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP37534.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP37534.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP37534.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP37534.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KQP37534.1}.
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DR EMBL; LMNA01000027; KQP37534.1; -; Genomic_DNA.
DR RefSeq; WP_056901696.1; NZ_LMNA01000027.1.
DR AlphaFoldDB; A0A0S9MX05; -.
DR STRING; 1736318.ASF44_14400; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000051759; 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; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02754; CCG; 2.
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; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT DOMAIN 54..282
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 651..680
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1017 AA; 108760 MW; D90B977869693FDD CRC64;
MHIDPASALL PAGTVLPPNE TCEALARRLR AETEGEVLFD AGSRGRYATD ASIYQIMPVG
VLVPKTARDV ALAIDIARDL KVPVLARGGG TSQCGQTTGA ALVIDNSKHL RRVLDIDVQA
RTATVEPGLV LDHLNAQLKP HGLWYPVDVS TSAQATLGGM AGNNSCGSRS IAYGNMVHNV
LGAQAWLSDG ELVNFGPVAG LGGRAAAIAD HVRKLAAQHS AEIAARWPKV MRRVAGYNLD
IFYNQSEKPY TADGSVNLAH LLVGSEGTLA VTRSLTLQLS ELPRAKVLGI VNFPSFHAAM
DAAQHIVKLG PTAVELVDRT MIELALANPA FRPTVETALI GKPAAILLVE FAGSEKAALL
PQLRQLVELM GDLGLPGSVV QMPDDAPQKN LWDVRKAGLN IMMSLKGDGK PVSFIEDCAV
PLEHLAEYTD ALTEVFAKYG SRGTWYAHAS VGTLHVRPIL DMRTDGGAKM RAIAEEASAL
VRKYKGAFSG EHGDGLCRGE WIEWQFGPAI NAAFRSIKQH LDPIGLLNPG KIIDPPKMDD
AALLRFAPPA SPRPYQRIEL KPVLDWSAWN VQADPVTEVT TAPGTGGDST GGFAKAVEMC
NNNGHCRKFD AGTMCPSYRV TRDEQHLTRG RANTLRLALS GQLGPDALAS EELHATMDLC
VGCKGCKRDC PTGVDMAKMK IEFLAHYKTQ HGHTLKDRLI ARLPDYAHRA SRLPWLMNLR
NRVPGAAWLG EKALGLSARR SLPAWRSDTF WRARDAQLFA GREATLAAAQ AGQKTAVLFV
DTFNGTFETE NALAAARVLK AAGYLLHTVE KAGGHHCCGR TYLASGMVDE ARAKAAALVD
ALAPFAQAGI AIVGLEPSCL LTLRDEALVM GLGDKAVSVS QQALLFEEFV AREAKAGRFS
IALQPAGKPI LLHGHCHQKA FGAVTPILDV LRLIPGAQPE LIESSCCGMA GSFGYEAAHY
AVSMQMAEAS LLPAVRQQPD AIVVADGTSC RHQIADGAQR EAVHVAVLLD RLRAARA
//
