ID R9AWP7_9GAMM Unreviewed; 407 AA.
AC R9AWP7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=SfnB family sulfur acquisition oxidoreductase {ECO:0000313|EMBL:EOR06623.1};
GN ORFNames=I593_02491 {ECO:0000313|EMBL:EOR06623.1};
OS Acinetobacter tandoii DSM 14970 = CIP 107469.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR06623.1, ECO:0000313|Proteomes:UP000016201};
RN [1] {ECO:0000313|EMBL:EOR06623.1, ECO:0000313|Proteomes:UP000016201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR06623.1,
RC ECO:0000313|Proteomes:UP000016201};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOR06623.1}.
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DR EMBL; AQFM01000039; EOR06623.1; -; Genomic_DNA.
DR RefSeq; WP_016167531.1; NZ_KE007367.1.
DR AlphaFoldDB; R9AWP7; -.
DR PATRIC; fig|1120927.3.peg.2426; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 6502068at2; -.
DR Proteomes; UP000016201; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR023922; S04_starv_induced_SfnB.
DR NCBIfam; TIGR04022; sulfur_SfnB; 1.
DR PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
FT DOMAIN 34..130
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 250..385
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 407 AA; 44753 MW; E193DB23B9A9F402 CRC64;
MTSFQTISPA QAAQLAPAHI IQSDAEALEI AHTLAEQFKH NAILRDAERI LPFDEIEAYS
KSGLWAITVP KQYGGAEVSS YTVAQIIALM SGVDGSIGQI PQNHFYALEV LRNTGTEQQK
QKLYQEVLQG ARFGNALAEF KTKNAAQKQT AISPTANGFI VNGEKFYCTG SLFAHRIPTL
VKDAHDREFL AFIPRNSEGL ELIDDWSGFG QRTTGSGTVK FHQVFVAAED VIPFDQAFQQ
PTLVGPFAQI MHAAIETGIA RAAFEETLIR VRQARPWIDS GVDAATQDPL TLLELGRVVA
DVRASEVLLK QAARSIDAAK PQPTEDNITQ ASLDVAKVRA HSSETALKAS SKLIELAGSR
GSQRVDGLDR FWRNARVHTL HDAARWKYYF IANYTLNGIR PPRRGTL
//
