ID   A0A2C8ZLN4_9MICO        Unreviewed;       810 AA.
AC   A0A2C8ZLN4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=HAD-superfamily subfamily IB hydrolase, TIGR01490 {ECO:0000313|EMBL:SOE65855.1};
GN   ORFNames=SAMN06296378_1631 {ECO:0000313|EMBL:SOE65855.1};
OS   Salinibacterium xinjiangense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Salinibacterium.
OX   NCBI_TaxID=386302 {ECO:0000313|EMBL:SOE65855.1, ECO:0000313|Proteomes:UP000219440};
RN   [1] {ECO:0000313|EMBL:SOE65855.1, ECO:0000313|Proteomes:UP000219440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.05381 {ECO:0000313|EMBL:SOE65855.1,
RC   ECO:0000313|Proteomes:UP000219440};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005928}.
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DR   EMBL; OCST01000003; SOE65855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C8ZLN4; -.
DR   Proteomes; UP000219440; Unassembled WGS sequence.
DR   GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd09071; FAR_C; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.20.1440.100; SG protein - dephosphorylation function; 1.
DR   InterPro; IPR026055; FAR.
DR   InterPro; IPR033640; FAR_C.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11011:SF45; FATTY ACYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR   Pfam; PF12710; HAD; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:SOE65855.1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219440}.
FT   DOMAIN          48..362
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   810 AA;  89480 MW;  16E83172B2086AFC CRC64;
     MTDASKTPVR KTPLAAKVPA KASTPRKPRA TPAAAVKNTI LTNEHVFITG GTGFVGQALL
     ERLLSSHPDT RMTLLVRGKG SLTGQARLAG LLRKPVFKNW IEAIGEEEAH RQFASRVTAH
     EGSLGNVGTL PDDIDVVIHS ASTVSFDPPI DEAFDTNVGG AHGVYGALLA SKSTPHVVHI
     STAYVGGIRK GIAPEASLTH EVDWRAEYEA AKSARIRVEL ESRQPEALRA QLSAAKARHG
     KTGPQAVAGF AETARNAWVR ERLVDYGRTR AESLGWTDVY TLTKAFAERA AEELWAQSGH
     RLSIVRPSII ESSLHHPFPG WIDGYKVADP LIIAYGRGQL PDFPGLPDSI LDVIPVDFVV
     NAALAVAARD AQPNEPKYYH VSSGASNPLP FHRMYENVNR YFTENPLPDG TGHITVPLWR
     FPGGVRVENA LARREKQAAT AEWLIEHLPT TPRTRAWLDV VTKGKHGLQK LRAFTELYRA
     YVQTEIIFDD ANTRALLLSL PEQIQETEGF DVTEIDWEDY FQKVHFPAVT TLTRAFGKRP
     AAKERATRAL PLRSDVVAIF DLEGTVLESN LVKQYLQLWA GSVPRKRVAH DLGNFAFSLP
     RYMRAERRDR GEFIRTFMRR YKGFRVSEIE GLVSGSFGRA MLRRALPDAL RRVQAHRDAG
     HRTVLVTGTI DLMVEPFLPY FDEVVAGSMH ERNGVLTGFL ADPPLVDEAR AAWLRHYAAK
     NGFDLEHSYG YGDSHADLVW LQLLGNPSVV NPDISLYRHA MEKHWNVLDW KRGSATSKPI
     LPMPTNNTAA ATDTAAPQAT PSTEGVGQTS
//