ID E6W4K4_DESIS Unreviewed; 967 AA.
AC E6W4K4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN OrderedLocusNames=Selin_2361 {ECO:0000313|EMBL:ADU67077.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU67077.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU67077.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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DR EMBL; CP002432; ADU67077.1; -; Genomic_DNA.
DR RefSeq; WP_013506950.1; NC_014836.1.
DR AlphaFoldDB; E6W4K4; -.
DR STRING; 653733.Selin_2361; -.
DR KEGG; din:Selin_2361; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG0511; Bacteria.
DR HOGENOM; CLU_306483_0_0_0; -.
DR InParanoid; E6W4K4; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002572; Chromosome.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR001249; AcCoA_biotinCC.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF4; BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR PRINTS; PR01071; ACOABIOTINCC.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT DOMAIN 34..617
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 847..937
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 967 AA; 108584 MW; A894ECFEA7C2D379 CRC64;
MAKKVDYYKK NPLIHRDRRL SKSSSKWVRS FSCEDLRPLI VCRGPIRKEA MDVYEEMGIN
HYGILLSEKD SIVYPNALAP ELRQLTDPSR VHRVPDYTGA SKEERVERIN QIIQIAKDNN
YDSIFAGYGF MAEDEEFVAA IEKAGLNFIG PNSITQARAG KKDEAKRTAL EVNVSVTPGI
DDVTVRTLLK KHPTRESLLA LVKSEGLSCD EKILGDSKVS LESLANHILF ASYAKGIDLF
SIDELCAQVQ VEVTEMFRKY PRSRVRLKAI GGGGGKGQRI LGASLLVAKE VTEEAIAKAA
AEAPGLVREV LNEVKANGVG DNKNVLVELN IEQTRHNEIQ LLGNGEWCVS LGGRDCSVQM
HEQKLLEVSV TKEGLEAAIE RARAAGNEKE VKSLQNDLTI LGRMEEEGAR FGQAVGLDSA
STFECIVDRD RHYFMEVNTR IQVEHRVTEL CYSLKFTNPD DPNDFFVVES LVEAMALLAR
HKKRVPKPER IKRFGASAEA RLNATDASLS PHAGGIIRYW SPPIEGEVRD DQGICLNNPD
TDVFMTYTVA GAYDSNIALL LTKGENRLES YQYLSRVLRK TKLRGTNLAT NLQFHYGLVN
WFIANGVNSK PTTRFVVPYL TLVGTLKEEA NKLDPVTAFL QMKKHYAARI GEMFADEPEA
QAAELKNISN ILDRKGTLLT RPMEVLLDDP HLLAGWLSLN KDNFRLEGGR VVWLRNPLVI
LDETYEYLNM SYDPKAPAAE IIWDHDNKVL QDALAFYSEL RKRLKLGKED FFKINELLQS
EKAPKGFDDS TWQQVRSAHF GYEAGVEILG TLFLIGDRTK FYDFCVDEDM DIIIPEHLND
PDLQARMKKI LVPPPATKAD EIVSPCGGMY YAQEAPGMPQ FIKEGDHFEK GQPLFIIEVM
KMFNKITAPF SGTVDKILIE GGEGVIVTKG QPLFKITPDE KFVEVDPKEL EKQRRECTIE
YLKAVLS
//
