ID Q4J6Z6_SULAC Unreviewed; 505 AA.
AC Q4J6Z6;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Gamma-aminobutyrate metabolism dehydratase/isomerase {ECO:0000313|EMBL:AAY81436.1};
DE EC=4.2.1.- {ECO:0000313|EMBL:AAY81436.1};
DE EC=5.3.3.3 {ECO:0000313|EMBL:AAY81436.1};
GN Name=abfD {ECO:0000313|EMBL:AAY81436.1};
GN OrderedLocusNames=Saci_2143 {ECO:0000313|EMBL:AAY81436.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779 {ECO:0000313|EMBL:AAY81436.1, ECO:0000313|Proteomes:UP000001018};
RN [1] {ECO:0000313|EMBL:AAY81436.1, ECO:0000313|Proteomes:UP000001018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
RC {ECO:0000313|Proteomes:UP000001018};
RX PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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DR EMBL; CP000077; AAY81436.1; -; Genomic_DNA.
DR RefSeq; WP_011278938.1; NZ_CP046615.1.
DR AlphaFoldDB; Q4J6Z6; -.
DR STRING; 330779.Saci_2143; -.
DR GeneID; 78442504; -.
DR KEGG; sai:Saci_2143; -.
DR PATRIC; fig|330779.12.peg.2148; -.
DR eggNOG; arCOG02143; Archaea.
DR HOGENOM; CLU_023920_1_0_2; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:AAY81436.1};
KW Lyase {ECO:0000313|EMBL:AAY81436.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001018}.
FT DOMAIN 5..274
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 282..477
FT /note="HpaB/PvcC/4-BUDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03241"
FT REGION 478..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 56630 MW; F5F79F6EC0FF9896 CRC64;
MVIRTGDQYV SSISKRSKVE IYVLGKEVKD VTKHPFLKPS VMSFKATFDA AWDEDTKELG
RAWSPYLEEE INRFNHIHRS PEDLAAKVKL LRKLSHKTGA CFQRCVGWDS LNTLNIVTKI
MANKGRTEPR DRFVEYLKYV QKNDLALAGA MTDVKGIRTL KPSQQPNKNA YLRVTEVTKD
GIYVSGAKAN ITGVAATEEM VVLPTRAMGP EDKDYAVAFA IPTDTEGIKI VVGRQINDAR
RMEEGEIDGL PYFYNHEGLV IFDNVFVPMN RVFLAGEWEY TGTLVEIFAA YHRQGYGGCK
AGLGDVIIGA SADLARQIGV EKAPHVQDKL TEMIFLTETM YSAGIAASLN AVKICDNCWW
VNPMHANVTK HLVARFPAQI SQLAIDIAGG MVGTAPSEWD LKNPKLKEYI MRYLQGVEDF
TAEDRLRMVR LIENVSMGVA FQIESIHGAG SPAAQRIMFS RLYDLDLARE ISKKLAGRKA
DLKMTTKPEP WRETQSEQEA KEHDK
//
