(data stored in SCRATCH zone)
SWISSPROT: Q3Z5B5_SHISS
ID Q3Z5B5_SHISS Unreviewed; 826 AA.
AC Q3Z5B5;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 08-MAY-2019, entry version 82.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:AAZ87047.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:AAZ87047.1};
GN Name=yafH {ECO:0000313|EMBL:AAZ87047.1};
GN OrderedLocusNames=SSON_0263 {ECO:0000313|EMBL:AAZ87047.1};
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87047.1, ECO:0000313|Proteomes:UP000002529};
RN [1] {ECO:0000313|EMBL:AAZ87047.1, ECO:0000313|Proteomes:UP000002529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87047.1,
RC ECO:0000313|Proteomes:UP000002529};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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DR EMBL; CP000038; AAZ87047.1; -; Genomic_DNA.
DR EnsemblBacteria; AAZ87047; AAZ87047; SSON_0263.
DR KEGG; ssn:SSON_0263; -.
DR HOGENOM; HOG000274434; -.
DR KO; K06445; -.
DR OMA; PIGKMEG; -.
DR Proteomes; UP000002529; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:InterPro.
DR Gene3D; 1.10.540.10; -; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR015396; DUF1974.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF09317; DUF1974; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 4: Predicted;
DR PRODOM; Q3Z5B5.
DR SWISS-2DPAGE; Q3Z5B5.
KW Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:AAZ87047.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9 30 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42 70 Helical. {ECO:0000256|SAM:Phobius}.
FT DOMAIN 159 244 Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT PF02771}.
FT DOMAIN 249 340 Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT PF02770}.
FT DOMAIN 372 516 Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT PF00441}.
FT DOMAIN 526 804 DUF1974. {ECO:0000259|Pfam:PF09317}.
SQ SEQUENCE 826 AA; 90568 MW; 199214E296CB482F CRC64;
MVRPPTSKGL FVMMILSILA TVVLLGALFY HRVSLFISSL ILLAWTAALG VAGLWSAWVL
VPLAIILVPF NFAPMRKSMI SAPVFRGFRK VMPPMSRTEK EAIDAGTTWW EGDLFQGKPD
WKKLHNYPQP RLTAEEQAFL DGPVEEACRM ANDFQITHEL ADLPPELWAY LKEHRFFAMI
IKKEYGGLEF SAYAQSRVLQ KLSGVSGILA ITVGVPNSLG PGELLQHYGT DEQKDHYLPR
LARGQEIPCF ALTSPEAGSD AGAIPDTGIV CMGEWQGQQV LGMRLTWNKR YITLAPIATV
LGLAFKLSDP EKLLGGAEDL GITCALIPTT TPGVEIGRRH FPLNVPFQNG PTRGKDVFVP
IDYIIGGPKM AGQGWRMLVE CLSVGRGITL PSNSTGGVKS VALATGAYAH IRRQFKISIG
KMEGIEEPLA RIAGNAYVMD AAASLITYGI MLGEKPAVLS AIVKYHCTHR GQQSIIDAMD
ITGGKGIMLG QSNFLARAYQ GAPIAITVEG ANILTRSMMI FGQGAIRCHP YVLEEMEAAK
NNDVNAFDKL LFKHIGHVGS NKVRSFWLGL TRGLTSSTPT GDATKRYYQH LNRLSANLAL
LSDVSMAVLD GSLKRRERIS ARLGDILSQL YLASAVLKRY DDEGRNEADL PLVHWGVQDA
LYQAEQAMDD LLQNFPNRVV AGLLNVVIFP TGRHYLAPSD KLDHKVAKIL QVPNATRSRI
GRGQYLTPSE HNPVGLLEEA LVDVIAADPI HQRICKELGK NLPFTRLDEL AHNALAKGLI
DKDEAAILVK AEESRLRSIN VDDFDPEELA TKPVKLPEKV RKVEAA
//
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