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Database: UniProt
Entry: S4XHB5_SORCE
LinkDB: S4XHB5_SORCE
Original site: S4XHB5_SORCE 
ID   S4XHB5_SORCE            Unreviewed;       416 AA.
AC   S4XHB5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Alanine acetyltransferase {ECO:0000313|EMBL:AGP32512.1};
GN   ORFNames=SCE1572_25405 {ECO:0000313|EMBL:AGP32512.1};
OS   Sorangium cellulosum So0157-2.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP32512.1, ECO:0000313|Proteomes:UP000014803};
RN   [1] {ECO:0000313|EMBL:AGP32512.1, ECO:0000313|Proteomes:UP000014803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So0157-2 {ECO:0000313|EMBL:AGP32512.1,
RC   ECO:0000313|Proteomes:UP000014803};
RX   PubMed=23812535; DOI=10.1038/srep02101;
RA   Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA   Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT   "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT   milieu.";
RL   Sci. Rep. 3:2101-2101(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP003969; AGP32512.1; -; Genomic_DNA.
DR   RefSeq; WP_020737001.1; NC_021658.1.
DR   AlphaFoldDB; S4XHB5; -.
DR   STRING; 1254432.SCE1572_25405; -.
DR   KEGG; scu:SCE1572_25405; -.
DR   PATRIC; fig|1254432.3.peg.5754; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_3_7; -.
DR   OrthoDB; 9774952at2; -.
DR   Proteomes; UP000014803; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08283; FDH_like_1; 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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42813:SF7; ALCOHOL DEHYDROGENASE (ZN-DEPENDENT)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transferase {ECO:0000313|EMBL:AGP32512.1};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..393
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   416 AA;  44218 MW;  0F59B507183ABD3F CRC64;
     MKAVVFHGVG DIRMDDIKEP KIKEPTDAIL RITASAICGT DLHFVRGTMP GMVPGTVLGH
     EAVGVVEETG KDVRNLKKGD RVVVPSTIAC GYCSYCRAAY YAQCDNANPN GKHAGTAFFG
     GPKMSGPFDG LQAEFARIPY ANVGLVKLPN GVSDDQAILL SDIFPTAYFG AELAEIRPGD
     TVAVFGCGPV GLFTIASAKL MGAGRIIAVD QVPDRLEMAR EQGAETVDFS AEDPLVALMR
     LTGGIGVDRA IDAVGVDAER PHDGPAHKQA KQDAKAFDLE VKQISPDART KGDTFRAGDG
     PSQVLQWAVR CVAKAGTISV IGVYPQTSRT FPIGEAMNKN LTLQMGNCNH RKYIPKLVDL
     VQTGQVDPTT IITKQAPLTS AIDAYKAFDR REAGWVKVEL RPSAAGAPAN LNRAVA
//
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