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Database: UniProt
Entry: C5NXS1_9BACL
LinkDB: C5NXS1_9BACL
Original site: C5NXS1_9BACL 
ID   C5NXS1_9BACL            Unreviewed;       163 AA.
AC   C5NXS1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151};
DE            EC=2.7.7.3 {ECO:0000256|HAMAP-Rule:MF_00151};
DE   AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00151};
DE   AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151};
DE            Short=PPAT {ECO:0000256|HAMAP-Rule:MF_00151};
GN   Name=coaD {ECO:0000256|HAMAP-Rule:MF_00151,
GN   ECO:0000313|EMBL:EER67646.1};
GN   ORFNames=GEMHA0001_0253 {ECO:0000313|EMBL:EER67646.1};
OS   Gemella haemolysans ATCC 10379.
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XI. Incertae Sedis; Gemella.
OX   NCBI_TaxID=546270 {ECO:0000313|EMBL:EER67646.1};
RN   [1] {ECO:0000313|EMBL:EER67646.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67646.1};
RA   Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA   Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EER67646.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67646.1};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Strausberg R.L., Nelson K.E.;
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and
CC       pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_00151,
CC       ECO:0000256|SAAS:SAAS00395140}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-
CC         CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC         ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00151, ECO:0000256|SAAS:SAAS01126069};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00151, ECO:0000256|SAAS:SAAS00834013};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00151,
CC       ECO:0000256|SAAS:SAAS00108991}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00151,
CC       ECO:0000256|SAAS:SAAS00109038}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151,
CC       ECO:0000256|SAAS:SAAS00108990}.
CC   -!- SIMILARITY: Belongs to the bacterial CoaD family.
CC       {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00580827}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EER67646.1}.
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DR   EMBL; ACDZ02000014; EER67646.1; -; Genomic_DNA.
DR   RefSeq; WP_003144971.1; NZ_ACDZ02000014.1.
DR   STRING; 546270.GEMHA0001_0253; -.
DR   EnsemblBacteria; EER67646; EER67646; GEMHA0001_0253.
DR   eggNOG; ENOG4108ZEF; Bacteria.
DR   eggNOG; COG0669; LUCA.
DR   OrthoDB; 1846503at2; -.
DR   BioCyc; GCF_000173915-HMP:GEMHA0001_RS06435-MONOMER; -.
DR   UniPathway; UPA00241; UER00355.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02163; PPAT; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00151; PPAT_bact; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR001980; PPAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21342:SF1; PTHR21342:SF1; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   PRINTS; PR01020; LPSBIOSNTHSS.
DR   TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109018};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109017};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109028};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00834014};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109023};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109019, ECO:0000313|EMBL:EER67646.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00108989, ECO:0000313|EMBL:EER67646.1}.
FT   DOMAIN        8    134       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND      11     12       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND      90     92       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND     125    131       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      11     11       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      19     19       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      43     43       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      75     75       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      89     89       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING     100    100       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   SITE         19     19       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   163 AA;  18514 MW;  237AADBD461C36C7 CRC64;
     MKRKIAIVPG SFDPITYGHI DIIKRSSELF DEIIVAILVN PDKKYLFSLD ERVEMIKETI
     KDIPNVRVDA FSGLLVNYAK KVGSSVIVRG LRAVSDFEYE MQLTFMNKAL DEGIETFYMM
     ANKQYSFISS SIVKGVSGFG ADLSKFVPKN VEERLEKKMK ERG
//
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