ID A0A087A2N4_9BIFI Unreviewed; 1508 AA.
AC A0A087A2N4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Activator of 2-hydroxyglutaryl-CoA dehydratase {ECO:0000313|EMBL:KFI53034.1};
DE EC=1.3.7.8 {ECO:0000313|EMBL:KFI53034.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:KFI53034.1};
GN ORFNames=BBIA_1010 {ECO:0000313|EMBL:KFI53034.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI53034.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI53034.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI53034.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KFI53034.1}.
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DR EMBL; JGYN01000003; KFI53034.1; -; Genomic_DNA.
DR STRING; 1437608.GCA_000771645_01738; -.
DR eggNOG; COG1924; Bacteria.
DR eggNOG; COG3580; Bacteria.
DR eggNOG; COG3581; Bacteria.
DR Proteomes; UP000029108; Unassembled WGS sequence.
DR GO; GO:0018522; F:benzoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 4.
DR InterPro; IPR002731; ATPase_BadF.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018709; CoA_activase_DUF2229.
DR InterPro; IPR008275; CoA_E_activase_dom.
DR NCBIfam; TIGR00241; CoA_E_activ; 1.
DR PANTHER; PTHR32329:SF4; ACTIVATOR OF 2-HYDROXYACYL-COA DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR32329; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1.
DR Pfam; PF01869; BcrAD_BadFG; 2.
DR Pfam; PF09989; DUF2229; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023014};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Oxidoreductase {ECO:0000313|EMBL:KFI53034.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029108}.
FT DOMAIN 19..277
FT /note="ATPase BadF/BadG/BcrA/BcrD type"
FT /evidence="ECO:0000259|Pfam:PF01869"
FT DOMAIN 349..603
FT /note="ATPase BadF/BadG/BcrA/BcrD type"
FT /evidence="ECO:0000259|Pfam:PF01869"
FT DOMAIN 750..968
FT /note="DUF2229"
FT /evidence="ECO:0000259|Pfam:PF09989"
FT REGION 624..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1080..1107
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 624..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1508
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1508 AA; 163288 MW; CFCC38E70CC742A3 CRC64;
MVNEAHTAAA RHDTKSLRVG LDIGSTTVKA VVLDQSDSLS DTIFSDYRRH HANVRATVAG
LLVDIHKELE GRGRGDEPIR LAITGSGGLA LADSMHVPFV QEVIAETEAI DKEYPAADVI
IELGGEDAKI TYLKPTPEQR MNGSCAGGTG AFIDQMATLL DTDASGLNEM AKSYENLYPI
ASRCGVFAKT DLQPLINDGA AKPDLAASIF TAVATQTIAG LASGRPIHGT VIFLGGPLFF
MSELRAAFQR ALDGKVDEFI VPTNAHLYVA YGAALQADMD KDDEGHHFEA RTCDDILKRL
DELKNLPSNT PTMPPLFPTE ADREAFNKRH HREHIHIGTL EGAHGPHFLG IDAGSTTIKA
TLVNDDREIV WSSYANNEGS PLTAAINIVK QIQSQLPQGA WIARSCATGY GEGLITTGLH
LDEGVVETMA HYRGAEMVSP GVTAVIDIGG QDMKYLAITD GVIDSIAVNE ACSSGCGSFL
QTFAMSMGLT IQEFTQKALA STHPVDLGSR CTVFMNSSVK QAQKEGASIE DIAAGLCYSV
VRNALYKVIK LRDSGELGDT VVVQGGTFLN DAVLRAFELL TEREVTRPNI AGLMGAYGAA
LTARMHYEDV ADDDHEHVLA DGTSAESTND TANVGANDTG DATSDVAADH ANEVVVDGVH
HTASSILTGD ELDHLSMTTE RDVCKLCQNH CKLTVTTFSD GSRFVTGNRC ERGGDAKKQR
SDRPNLYDYK YKRCFAYRRL TDKKATRGEI GIPRALNMYE NYPFWFTLLT SLGFKVMISG
RSSHELFETG IESIASENIC YPAKLVHGHI KWLLNKGVKT IFYPCVSYED NLVPNTDNHY
NCPVVANYPL VVGANMPELR EDGVRYMHPY FNLANHELMV DRIVEEFAWA NVTREEAETA
VKAAYAEDKV FKNDVQQEGL KALAYMKEHG CRGIVLAGRP YHVDPEINHG IPETICSLGM
VVLSEDSICE LQPGQKLDLT EFLSAGEEDP RKKNANGFRH VGDRKVSVNR MPLRVTNQWA
YHSRLYAAAH FVASYPGLEL VQLNSFGCGL DAITTDQVSE ILADKADVYT LLKIDEVSNL
GAAKIRLRSL KAAVEERERN KAKAVAAVSA AHGAGAAGAG ATGSSAAQLV GKQDQTIVAA
PSAAEIKARE AAQAKAQADL AAAETQLAAA KEQLAAAQAA VKAAEAKRAA ADSAVADDET
AQSAAPKSTG FRKTGSQAPT PGRQVLLDTT MAANPKLTES VRRASRLAAQ RDIEAAVNAK
TVLAGSDGTV DTPGKTAQKA KSGHNNATMS RYAHRQKFVK DMKKDYTIVA PQMSPIHMSL
VEAVIRSGGY KFDILKHASR GDVETGLKYV NNDACYPAIM VIGQLIDAII QGKYDPDHVA
LAITQTGGMC RATNYFGLIR KALIDAGYPQ IPVIAISTQG LEDNPGFKAT PVLLHRAIKA
LILGDLLMKC LYRVRPYEVE PGAANRLYEQ WDVIVRETLE HHASPRPRPR RRGSRKRTCR
IRYSPRRS
//
