ID F9ZDI5_9PROT Unreviewed; 458 AA.
AC F9ZDI5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ADZ25476.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:ADZ25476.1};
GN ORFNames=NAL212_0532 {ECO:0000313|EMBL:ADZ25476.1};
OS Nitrosomonas sp. AL212.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ25476.1, ECO:0000313|Proteomes:UP000001629};
RN [1] {ECO:0000313|EMBL:ADZ25476.1, ECO:0000313|Proteomes:UP000001629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ25476.1,
RC ECO:0000313|Proteomes:UP000001629};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002552; ADZ25476.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZDI5; -.
DR STRING; 153948.NAL212_0532; -.
DR KEGG; nit:NAL212_0532; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_4; -.
DR Proteomes; UP000001629; Chromosome.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000313|EMBL:ADZ25476.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001629}.
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 458 AA; 49457 MW; 6339DB9B39EC29D4 CRC64;
MLSANLLTEL QRTFPPDRFY TDPVDCYSYA YDNSRKIFPP DAVLFPLTTE EVRQIVSLCN
KYHVPLIPRG RGTGTAGGSL PEFGGIALSM ERMLNIISID PANRIIVAEP GVLNQTVQDA
AKPHGFFWPP DPSSAQFSSI GGNIATSAGG PHAVKYGTTR EHVLGLKAVT GTGDLITTGC
YTTKGVVGYD LTRLLIGSEG TLAVITEATL KLSALPTAVA GITAHFNDLS SCTQAIVNIM
ALPQLPSALE FLDAGSLNLI RGRYPNMLPV DTHAMLMIEV DGSDQDISTS ITAILEACRS
NGLINAQQAN DTTALWQARK ALSPLLKEIA PKKINEDVVV PVTTLPQFLA GLEKLSDHYQ
LHNVNFGHAG NGNIHVNLLI NPDDKEEVAR AERCLDEIFD LVIGLRGTLS GEHGIGSEKR
AFVTKEIDRV TLDLMRNIKQ VFDPNNILNP GKVFPLTP
//
