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Multifunctional fusion protein [Includes: Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (7,8-diaminononanoate synthase) (Diaminopelargonic acid synthase) (DANS) (DAPA AT) (DAPA aminotransferase); Biotin synthase (EC 2.8.1.6)]

 F7L9D1_BACOV            Unreviewed;       804 AA.
F7L9D1;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
23-MAY-2018, entry version 41.
SubName: Full=Biotin synthase {ECO:0000313|EMBL:EGM95474.1};
Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
Synonyms=bioB {ECO:0000256|HAMAP-Rule:MF_01694};
ORFNames=HMPREF1017_01814 {ECO:0000313|EMBL:EGM95474.1};
Bacteroides ovatus 3_8_47FAA.
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
Bacteroides.
NCBI_TaxID=665954 {ECO:0000313|EMBL:EGM95474.1, ECO:0000313|Proteomes:UP000003356};
[1] {ECO:0000313|EMBL:EGM95474.1, ECO:0000313|Proteomes:UP000003356}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=3_8_47FAA {ECO:0000313|EMBL:EGM95474.1,
ECO:0000313|Proteomes:UP000003356};
The Broad Institute Genome Sequencing Platform;
Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G.,
Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C.,
Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A.,
Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C.,
Wortman J., Nusbaum C., Birren B.;
"The Genome Sequence of Bacteroides ovatus 3_8_47FAA.";
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin
by the insertion of a sulfur atom into dethiobiotin via a radical-
based mechanism. {ECO:0000256|HAMAP-Rule:MF_01694}.
-!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
(KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
animotransferase known to utilize SAM as an amino donor.
{ECO:0000256|HAMAP-Rule:MF_00834}.
-!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S-
adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin +
(sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2
oxidized [2Fe-2S] ferredoxin. {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00190209}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
diaminononanoate. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00370166}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01694}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
Rule:MF_00834}.
-!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin
synthase family. {ECO:0000256|HAMAP-Rule:MF_01694}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EGM95474.1}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; ACWH01000008; EGM95474.1; -; Genomic_DNA.
RefSeq; WP_004304124.1; NZ_GL945020.1.
ProteinModelPortal; F7L9D1; -.
EnsemblBacteria; EGM95474; EGM95474; HMPREF1017_01814.
PATRIC; fig|665954.3.peg.1854; -.
OrthoDB; POG091H01IB; -.
BioCyc; BOVA665954-HMP:GM9L-1835-MONOMER; -.
UniPathway; UPA00078; UER00160.
UniPathway; UPA00078; UER00162.
Proteomes; UP000003356; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_00834; BioA; 1.
HAMAP; MF_01694; BioB; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR010722; BATS_dom.
InterPro; IPR034416; BATS_domain_containing.
InterPro; IPR005815; BioA.
InterPro; IPR002684; Biotin_synth/BioAB.
InterPro; IPR006638; Elp3/MiaB/NifB.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
InterPro; IPR007197; rSAM.
Pfam; PF00202; Aminotran_3; 1.
Pfam; PF06968; BATS; 1.
Pfam; PF04055; Radical_SAM; 1.
SFLD; SFLDG01060; BATS_domain_containing; 1.
SFLD; SFLDG01278; biotin_synthase_like; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
SMART; SM00876; BATS; 1.
SMART; SM00729; Elp3; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00508; bioA; 1.
TIGRFAMs; TIGR00433; bioB; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
3: Inferred from homology;
2Fe-2S {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00063334};
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00911672};
Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00063242};
Complete proteome {ECO:0000313|Proteomes:UP000003356};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
Iron {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00063334,
ECO:0000256|SAAS:SAAS00911672};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00063334, ECO:0000256|SAAS:SAAS00911672};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00063334, ECO:0000256|SAAS:SAAS00911672};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01694,
ECO:0000256|SAAS:SAAS00911682};
Transferase {ECO:0000256|HAMAP-Rule:MF_00834}.
DOMAIN 115 320 Elp3. {ECO:0000259|SMART:SM00729}.
DOMAIN 291 382 BATS. {ECO:0000259|SMART:SM00876}.
REGION 491 492 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00834}.
REGION 688 689 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00834}.
METAL 125 125 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01694}.
METAL 129 129 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01694}.
METAL 132 132 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01694}.
METAL 169 169 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694}.
METAL 201 201 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694}.
METAL 261 261 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694}.
METAL 331 331 Iron-sulfur 2 (2Fe-2S).
{ECO:0000256|HAMAP-Rule:MF_01694}.
BINDING 431 431 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 524 524 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 625 625 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 654 654 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 687 687 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00834}.
BINDING 771 771 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
SITE 396 396 Participates in the substrate recognition
with KAPA and in a stacking interaction
with the adenine ring of SAM.
{ECO:0000256|HAMAP-Rule:MF_00834}.
MOD_RES 654 654 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_00834}.
SEQUENCE 804 AA; 90081 MW; 1550EF5D88CFC8EC CRC64;
MKQQRHIQTT RTLLSRFRYW GRKNYAAFAS MGREFQIGHL HTNVVDVALR KQNAAQTIPY
HTFMTLQEIK DQVLAGIDIS PDQAAWLANM ADSEALYAAA HEITVARASH EFDMCSIINA
KSGRCPENCK WCAQSSHYQT KAEIYDLLPA EECLRQAQYN EAQDVNRFSL VTSGRKPSPK
QITQLCDTVR YMRRHSSIQL CASLGLLNEE ELRSLHEAGI TRYHCNLETA PSYFSKLCST
HTQEQKLATL DAARRVGMDI CCGGIIGMGE TMEQRIEFAF TLAELNVQSI PINLLSPIPG
TPLENEQPLS EEEILKTIAL FRFINPTAFL RFAGGRSQLS SEAMHKALYI GINSAIVGDL
LTTLGSKVSE DKKMIQEEGY HFADSQFDRE HIWHPYTSTT DPLPVYKVKR ADGATITLED
GRTLIDGMSS WWCAVHGYNH PVLNQAAKEQ LDKISHVMFG GLTHDPAIEL GKLLLPLVPS
SMQKIFYADS GSVAVEVALK MAVQYWYAAG KPEKNNFVTI RSGYHGDTWN AMSVCDPVTG
MHSLFGSALP VRYFVPSPTS RFDGEWNPKD ILPLQEMIEK HSKELAALIL EPVVQGAGGM
WFYHPQYLRE AEKLCRKHDI LLIFDEIATG FGRTGKLFAW EHAGVEPDIM CIGKALTGGY
MTLSAVLTSN RIADTISNHA PGAFMHGPTF MGNPLACAVA CASVRLLLES GWQKNVKRIE
TQLKEELAPA REFPEVADVR ILGAIGVIEM KRPVNMAYMQ RRFVEERIWV RPFGKLVYLM
PPFIITSEQL SKLTSGLLKV IQKR


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