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Database: UniProt
Entry: A0A401Y8Y6_9ACTN
LinkDB: A0A401Y8Y6_9ACTN
Original site: A0A401Y8Y6_9ACTN 
ID   A0A401Y8Y6_9ACTN        Unreviewed;       428 AA.
AC   A0A401Y8Y6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Crotonyl-CoA carboxylase/reductase {ECO:0000313|EMBL:GCD91117.1};
GN   Name=adhP {ECO:0000313|EMBL:GCD91117.1};
GN   ORFNames=NLS1_31230 {ECO:0000313|EMBL:GCD91117.1};
OS   Nocardioides sp. LS1.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1027620 {ECO:0000313|EMBL:GCD91117.1, ECO:0000313|Proteomes:UP000288271};
RN   [1] {ECO:0000313|EMBL:GCD91117.1, ECO:0000313|Proteomes:UP000288271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS1 {ECO:0000313|EMBL:GCD91117.1,
RC   ECO:0000313|Proteomes:UP000288271};
RA   Morimura H., Sato I., Uesaka K.;
RT   "Draft Genome sequence of the deoxynivalenol-degrading actinomycete
RT   Nocardioides sp. strain LS1, isolated from wheat leaves in Japan.";
RL   Submitted (NOV-2018) 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:GCD91117.1}.
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DR   EMBL; BIFF01000005; GCD91117.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401Y8Y6; -.
DR   OrthoDB; 9790818at2; -.
DR   Proteomes; UP000288271; 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   Reference proteome {ECO:0000313|Proteomes:UP000288271};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          46..410
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  45438 MW;  AD397D9629181F72 CRC64;
     MASSHQAERN SVVTPGVEPT PVGQLPPVGQ VPSHMHAQLV RQDRFGDPAT AFVAEVVPTP
     DIRPDEVLIG VMAAGINYNN VWAARGYPVD QIATRQRRGE TEDFHIGGSD ASGIVYAVGG
     EVNGIEVGDH VVTHPGVWDA DDAWIARGKD QMTAPTARIY GYDTNYGSFG QFTRVQAHQV
     LPKAAHLTWE EAAAPTLVGT TAYRMLHGWQ GNVVSEGDVV LVWGGSGGLG SQAIQLARLA
     GAIPVAVVSE PERGAYAEKL GAAGWINRRD FNHWGVPPLV DDAAGQKAWT AEARTFGKRI
     WDIVGSRQDP AIVFEHPGAA TIPTSIFVCE TGGMVVICAG TTGYDAMVDL RYHWTRQKRL
     QGSHGTNDAE ARAYNDLVLA GAIDPALGRT IRFEDIPGAH AAMGRGEEVF GNVSALVGAP
     HPGAGADL
//
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