ID K6I633_9LEPT Unreviewed; 401 AA.
AC K6I633;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Crotonyl-CoA reductase {ECO:0000313|EMBL:EKO79055.1};
GN Name=ccrA {ECO:0000313|EMBL:EKO79055.1};
GN ORFNames=LEP1GSC068_3902 {ECO:0000313|EMBL:EKO79055.1};
OS Leptospira sp. Fiocruz LV3954.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193012 {ECO:0000313|EMBL:EKO79055.1, ECO:0000313|Proteomes:UP000002809};
RN [1] {ECO:0000313|EMBL:EKO79055.1, ECO:0000313|Proteomes:UP000002809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz LV3954 {ECO:0000313|EMBL:EKO79055.1,
RC ECO:0000313|Proteomes:UP000002809};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Selengut J.D., Sanka R., DePew J.,
RA Ko A.I., Reis M.G., Ribeiro G.S., Wunder E.Jr., Vinetz J.M., Sutton G.G.,
RA Nelson W.C., Fouts D.E.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:EKO79055.1}.
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DR EMBL; AKWV02000029; EKO79055.1; -; Genomic_DNA.
DR AlphaFoldDB; K6I633; -.
DR PATRIC; fig|1193012.3.peg.1323; -.
DR Proteomes; UP000002809; Unassembled WGS sequence.
DR GO; GO:0043880; F:crotonyl-CoA reductase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08246; crotonyl_coA_red; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR010085; Crot_CoA_red.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR NCBIfam; TIGR01751; crot-CoA-red; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 19..382
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 401 AA; 44085 MW; D401C4DA0AABB836 CRC64;
MGQVPKKMYA QVVRPERYGD PITAIQEELI DVPEIAPDEV LVAVMAAGVN YNNVWAALGF
PVDVIGARNK KGEPEKFHIG GSDASGIVYK VGSEVKNVKV GDEVVLHCGI WDKNDPWVKA
GKDPMFAPSQ LIWAYETNWG SFAQFCKVQD HQCLPKPKHL SWEEAAAYML VGATAYRMLH
HWKPNDVQKD DVVLIWGGAG GLGAMAIQIV KAAGGIPIAV VSEDDKIDFC KKLGAAGVIN
RKKFNHWGAL TSEINKMEKF VEWTKSAREF GKAIWDIAGK GNNPKIVFEH PGETTIPTSM
FVCETGGMVV ICAGTTGYNA TVDLRYLWMR QKRLQGSHFA NDENSKGLND LVIDKKVDPC
LSKTFAWNET AHSHQLMKEN KHPAGNMSIL VGADKPGQGK K
//
