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Multifunctional fusion protein [Includes: Bifunctional ligase/repressor BirA (Biotin--[acetyl-CoA-carboxylase] ligase) (Biotin--protein ligase) (Biotin-[acetyl-CoA carboxylase] synthetase) (EC 6.3.4.15); Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase)]

 A0A1Z8U6B8_9BACT        Unreviewed;       606 AA.
A0A1Z8U6B8;
22-NOV-2017, integrated into UniProtKB/TrEMBL.
22-NOV-2017, sequence version 1.
18-JUL-2018, entry version 8.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00978, ECO:0000256|HAMAP-Rule:MF_01274};
Includes:
RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000256|HAMAP-Rule:MF_00978};
AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000256|HAMAP-Rule:MF_00978};
AltName: Full=Biotin--protein ligase {ECO:0000256|HAMAP-Rule:MF_00978};
AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000256|HAMAP-Rule:MF_00978};
EC=6.3.4.15 {ECO:0000256|HAMAP-Rule:MF_00978};
Includes:
RecName: Full=Type III pantothenate kinase {ECO:0000256|HAMAP-Rule:MF_01274};
EC=2.7.1.33 {ECO:0000256|HAMAP-Rule:MF_01274};
AltName: Full=PanK-III {ECO:0000256|HAMAP-Rule:MF_01274};
AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_01274};
Name=coaX {ECO:0000256|HAMAP-Rule:MF_01274};
Synonyms=birA {ECO:0000256|HAMAP-Rule:MF_00978};
ORFNames=CBC16_03955 {ECO:0000313|EMBL:OUU42454.1};
Verrucomicrobia bacterium TMED56.
Bacteria; Verrucomicrobia; unclassified Verrucomicrobia.
NCBI_TaxID=1986792 {ECO:0000313|EMBL:OUU42454.1};
[1] {ECO:0000313|EMBL:OUU42454.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TMED56 {ECO:0000313|EMBL:OUU42454.1};
Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
"290 Metagenome-assembled Genomes from the Mediterranean Sea: a
resource for marine microbiology.";
Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase
and a repressor. {ECO:0000256|HAMAP-Rule:MF_00978}.
-!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384421}.
-!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'-
phosphopantothenate. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384435}.
-!- CATALYTIC ACTIVITY: ATP + biotin + [biotin carboxyl-carrier
protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier
protein]-N(6)-biotinyl-L-lysine. {ECO:0000256|HAMAP-
Rule:MF_00978}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|SAAS:SAAS00611758};
-!- COFACTOR:
Name=NH4(+); Xref=ChEBI:CHEBI:28938;
Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
Note=A monovalent cation. Ammonium or potassium.
{ECO:0000256|HAMAP-Rule:MF_01274};
-!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
(R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384485}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00701620}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384519}.
-!- SIMILARITY: Belongs to the biotin--protein ligase family.
{ECO:0000256|HAMAP-Rule:MF_00978}.
-!- SIMILARITY: Belongs to the type III pantothenate kinase family.
{ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00701623}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OUU42454.1}.
-----------------------------------------------------------------------
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EMBL; NHDJ01000046; OUU42454.1; -; Genomic_DNA.
UniPathway; UPA00241; UER00352.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009305; P:protein biotinylation; IEA:UniProtKB-UniRule.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd16442; BPL; 1.
Gene3D; 1.10.10.10; -; 1.
HAMAP; MF_00978; Bifunct_BirA; 1.
HAMAP; MF_01274; Pantothen_kinase_3; 1.
InterPro; IPR030855; Bifunct_BirA.
InterPro; IPR004408; Biotin_CoA_COase_ligase.
InterPro; IPR003142; BPL_C.
InterPro; IPR004143; BPL_LPL_catalytic.
InterPro; IPR013196; HTH_11.
InterPro; IPR008988; Transcriptional_repressor_C.
InterPro; IPR004619; Type_III_PanK.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR34265; PTHR34265; 1.
Pfam; PF02237; BPL_C; 1.
Pfam; PF03099; BPL_LplA_LipB; 1.
Pfam; PF08279; HTH_11; 1.
Pfam; PF03309; Pan_kinase; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF50037; SSF50037; 1.
TIGRFAMs; TIGR00671; baf; 1.
TIGRFAMs; TIGR00121; birA_ligase; 1.
PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00978,
ECO:0000256|SAAS:SAAS00088442};
Biotin {ECO:0000256|HAMAP-Rule:MF_00978};
Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088444};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088451};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_00978};
Kinase {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088438};
Ligase {ECO:0000256|HAMAP-Rule:MF_00978, ECO:0000313|EMBL:OUU42454.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00978,
ECO:0000256|SAAS:SAAS00088442};
Potassium {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00461364};
Repressor {ECO:0000256|HAMAP-Rule:MF_00978};
Transcription {ECO:0000256|HAMAP-Rule:MF_00978};
Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00978};
Transferase {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088438}.
DOMAIN 100 285 BPL/LPL catalytic.
{ECO:0000259|PROSITE:PS51733}.
DNA_BIND 45 64 H-T-H motif. {ECO:0000256|HAMAP-
Rule:MF_00978}.
NP_BIND 362 369 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
REGION 116 118 Biotin binding. {ECO:0000256|HAMAP-
Rule:MF_00978}.
REGION 144 146 Biotin binding. {ECO:0000256|HAMAP-
Rule:MF_00978}.
REGION 453 456 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01274}.
ACT_SITE 455 455 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01274}.
METAL 475 475 Monovalent cation. {ECO:0000256|HAMAP-
Rule:MF_01274}.
BINDING 140 140 Biotin. {ECO:0000256|HAMAP-
Rule:MF_00978}.
BINDING 212 212 Biotin. {ECO:0000256|HAMAP-
Rule:MF_00978}.
BINDING 446 446 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01274}.
BINDING 478 478 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
BINDING 533 533 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01274}.
SEQUENCE 606 AA; 67148 MW; 69DFB376D3AB5F1A CRC64;
MPNYPTGKRK RIKAGKIRGL SKKVREPNSF VLKMLLNAAP YYVSGSILAE KLNMSRVGVW
SRIDKLRKSG LTIEASQNLG YRLAGEPNQY SLPLIKAWLS ELRKTCDIFT HDQIDSTNSE
VERLLANGQK APFAVLANKQ LTGRGRLGRS WHSPKGGNLY LSIGFRPNIN AIRIRNFTLW
QGIKICKFXQ EFIGSDKIKV KWPNDLYYEG KKIAGMLTEA SIDCERIXTL VFGLGMNVNI
PSKQYPSTLS KSSISLQSLV GGQIRLHELS AKIIKVVLQC YENSIQENFK SNLTDEWKEV
DAIYGKKVEI KLGKEIFTGK ALGVDQSGNL RIKLRNGRIK IIQSGEVIEK LXARMSXIQC
LDIGNTRTKL GVFKGTKMXK IVSFETKKLS AEANFFDSVI IEQNGPLCYC SVVPFVERIL
NKNLSNFTQE IICVNSLNRA NLPXSYPTPE EIGADRIANA IAAFNILTLP AIVIDIGTAT
TFDVISCKGG YEGGVILPGP QGFLDYLHDS TALLPRVELS TNSNLSNSYG KSTKEAMLLG
VRLGYKTMVG EIIKKISHQI NLLDKQSVSV VLTGGSSTNF DLGSFPIHEN LTLQGLKLAF
EMRSSL


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