ID D7A537_STAND Unreviewed; 506 AA.
AC D7A537;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Vinylacetyl-CoA Delta-isomerase {ECO:0000313|EMBL:ADH89925.1};
DE EC=5.3.3.3 {ECO:0000313|EMBL:ADH89925.1};
GN OrderedLocusNames=Snov_2630 {ECO:0000313|EMBL:ADH89925.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Ancylobacter.
OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH89925.1, ECO:0000313|Proteomes:UP000006633};
RN [1] {ECO:0000313|EMBL:ADH89925.1, ECO:0000313|Proteomes:UP000006633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
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DR EMBL; CP002026; ADH89925.1; -; Genomic_DNA.
DR RefSeq; WP_013167429.1; NC_014217.1.
DR AlphaFoldDB; D7A537; -.
DR STRING; 639283.Snov_2630; -.
DR KEGG; sno:Snov_2630; -.
DR eggNOG; COG2368; Bacteria.
DR HOGENOM; CLU_023920_2_1_5; -.
DR OrthoDB; 7233724at2; -.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0050393; F:vinylacetyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.3140.10; 4-hydroxybutyryl-coa dehydratase, domain 1; 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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR PANTHER; PTHR36117; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR36117:SF3; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR PIRSF; PIRSF000331; HpaA_HpaB; 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;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Isomerase {ECO:0000313|EMBL:ADH89925.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..267
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 275..473
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT REGION 141..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 56750 MW; 1E4DD326C831F538 CRC64;
MIRTGAQYLE SIRDGREVYV NGERVKDVPS HPMFKPLVDI RARIYDMQWD AKTRDVMTFT
QDGEVNGIGN KLPITQQDWW DKRRATDCVL QDVGGVVTRV GDEAVGEMWS LFDGQDVLNE
VDPRFSENIR NHIDKVLHTD PFHVSANTDP KGDRSKPPQE QDPDMLLHVV KETDAGIVVR
GAKFETAAAY ANQAFTKPTI ANWGDSAYSD YAVGFICDLG SPGIKFICRT GFAGQKPIED
YPVSNRFDEV DALVIFDDVL IPWENVLFYR HTRAAMFIRA TLHRYSAFAF VQRNLMFADM
LIGAALFNVR QTGLDRQQAV QEKLSRLAVY REGINAHLTA AVTLAERSPG GLLMPNQSLL
YAGRVLACSQ LHEIMHVARE LCGGQICVTP DAAAFAHPDT KPWLDKFYTV NEDWVADDRR
KLLAFARDIL NSDYAGHRLT FQLFAQSPPF AHLAAVYRNF DWDGPLELVK KSAGLSDRVL
GTATRTAGDS AISRWFDPSM NRAAAE
//
