Q12627

PR
Gene name
DLD1 (DLD, KLLA0E19789g)
Protein name
D-lactate dehydrogenase [cytochrome], mitochondrial
Names
D-lactate ferricytochrome C oxidoreductase, D-LCR
Species
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
KEGG Pathway
kla:KLLA0_E19691g
EC number
1.1.2.4: With a cytochrome as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-120 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q12627

Entry ID Method Resolution Chain Position Source
AF-Q12627-F1 Predicted AlphaFoldDB

No variants for Q12627

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q12627

No associated diseases with Q12627

3 regional properties for Q12627

Type Name Position InterPro Accession
domain FAD-binding oxidoreductase/transferase, type 4, C-terminal 324 - 566 IPR004113
domain FAD linked oxidase, N-terminal 144 - 283 IPR006094
domain FAD-binding domain, PCMH-type 139 - 320 IPR016166

Functions

Description
EC Number 1.1.2.4 With a cytochrome as acceptor
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

2 GO annotations of molecular function

Name Definition
D-lactate dehydrogenase (cytochrome) activity Catalysis of the reaction: (R)-lactate + 2 [Fe(III)cytochrome c] = 2 [Fe(II)cytochrome c] + 2 H+ + pyruvate.
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.

1 GO annotations of biological process

Name Definition
lactate catabolic process The chemical reactions and pathways resulting in the breakdown of lactate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFRFVGRSGF ALRGSLQLRK DVLRSRTTAV AKRHYSSSNG NNGGGFSSAI LSVLGGSLIG
70 80 90 100 110 120
GGFVAYALGS QFEKEKSVSD LSIARLEDLD SPEYCDKETF AKALVELKDV LENDPENFTV
130 140 150 160 170 180
AKDDLDAHSD TYFNSHHAEA NQRPEIVLYP RNTEDVSKLL KICHKYSIPV IPFSGGTSLE
190 200 210 220 230 240
GHFLPTRPGS CVVLDISKYL NKIIQLNKED LDVVVQGGVP WEELNEYLND HGLLFGCDPG
250 260 270 280 290 300
PGAQIAGCIA NSCSGTNAYR YGTMKENVVN ITMCMADGTI VKTKRRPRKS SAGYNLNGLI
310 320 330 340 350 360
IGSEGTLGIV TEATIKCHVR STFETVAVVP FPTVSDAASC SSHLIQAGIQ LNAMELLDDN
370 380 390 400 410 420
MMKIINQSGA TSKDNWVESP TLFFKIGGRS EQIIQEVIKE VEKIASQHNN TKFEFATDED
430 440 450 460 470 480
SKLELWEARK VALWSTIDTG RKTNPDANIW TTDVAVPISK FADVINATKE EMNASGLLTS
490 500 510 520 530 540
LVGHAGDGNF HAFIIYNTEQ RKTAETIVEN MVKRAIDAEG TCTGEHGVGI GKRDYLLEEV
550 560 570
GEDTVAVMRK LKLALDPKRI LNPDKIFKID PNDHQH