ID   A0A091KRS5_9GRUI        Unreviewed;       466 AA.
AC   A0A091KRS5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Ubiquitin-conjugating enzyme E2 variant 3 {ECO:0000313|EMBL:KFP42163.1};
DE   Flags: Fragment;
GN   ORFNames=N324_06764 {ECO:0000313|EMBL:KFP42163.1};
OS   Chlamydotis macqueenii (Macqueen's bustard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX   NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP42163.1, ECO:0000313|Proteomes:UP000053330};
RN   [1] {ECO:0000313|EMBL:KFP42163.1, ECO:0000313|Proteomes:UP000053330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP42163.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate
CC       and lactate with concomitant interconversion of NADH and NAD(+).
CC       {ECO:0000256|ARBA:ARBA00033729}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC         Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00033677};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC         Evidence={ECO:0000256|ARBA:ARBA00033677};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC         Evidence={ECO:0000256|ARBA:ARBA00033677};
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DR   EMBL; KK752249; KFP42163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091KRS5; -.
DR   Proteomes; UP000053330; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   CDD; cd05293; LDH_1; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR008883; UEV_N.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF32; UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 3; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   Pfam; PF05743; UEV; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS51322; UEV; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053330}.
FT   DOMAIN          1..131
FT                   /note="UEV"
FT                   /evidence="ECO:0000259|PROSITE:PS51322"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP42163.1"
FT   NON_TER         466
FT                   /evidence="ECO:0000313|EMBL:KFP42163.1"
SQ   SEQUENCE   466 AA;  50843 MW;  F4160AD53848F4F3 CRC64;
     QYKFRDLTIE ELKNVTKTYP NFTFSMNTYT FKDGSQKDLL NFSGTVPVKY GNSYNIPIHL
     WILDSHPFAP PICFLKPTAN MGISVGKHVD ANGRIYLPYL QNWSHPKSTV IGLIKEMIAK
     FEEELPLYSL SSSDADRQSE LLSYIAKITE GEADVKSKSK IGGGKNEGCF NKITVVGAGD
     LGIACVLAVA AKGSTDKVVL LDLSEGVAKG GTMDLEIFAL PNVEISKDFS ASADSKVVVL
     TVNSLGNAQT YLDVIQSNVD LFREIIPAIS HYSQNAVLLV ASHPVEVMTY VSWKLSAFPK
     SRVIGVGANL DTERFQYILT NHLKAQVLAK GAWIIGEQGE DKVPSWTSCN LVVNQTEAMA
     ACNSREKVAN RAMEVLKGKG QRSWSVGLSV ADLTDSILKD KRKIHSVSTL AKGCCNINSE
     VFLSLPCLLG TNGVIEMVKL EEDPLAQKKL QSSAGSINDL QQQLKL
//