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Database: UniProt
Entry: A0A132PD75_9MYCO
LinkDB: A0A132PD75_9MYCO
Original site: A0A132PD75_9MYCO 
ID   A0A132PD75_9MYCO        Unreviewed;       619 AA.
AC   A0A132PD75;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   18-JUL-2018, entry version 20.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00062, ECO:0000256|HAMAP-Rule:MF_00065};
DE   Includes:
DE     RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00062};
DE              EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00062};
DE     AltName: Full=ATP-sulfurylase large subunit {ECO:0000256|HAMAP-Rule:MF_00062};
DE     AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00062};
DE              Short=SAT {ECO:0000256|HAMAP-Rule:MF_00062};
DE   Includes:
DE     RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE              EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065};
DE     AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE     AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
DE     AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
GN   Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN   Synonyms=cysN {ECO:0000256|HAMAP-Rule:MF_00062};
GN   ORFNames=AFM11_33610 {ECO:0000313|EMBL:KWX19922.1};
OS   Mycolicibacterium wolinskyi.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX19922.1, ECO:0000313|Proteomes:UP000070612};
RN   [1] {ECO:0000313|EMBL:KWX19922.1, ECO:0000313|Proteomes:UP000070612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC_01 {ECO:0000313|EMBL:KWX19922.1,
RC   ECO:0000313|Proteomes:UP000070612};
RA   de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA   Limbago B.M., Noble-Wang J.;
RT   "A draft genome sequence of Mycobacterium wolinskyi.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
CC       phosphoadenylyl sulfate. {ECO:0000256|HAMAP-Rule:MF_00065,
CC       ECO:0000256|SAAS:SAAS00774039}.
CC   -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
CC       sulfate. {ECO:0000256|HAMAP-Rule:MF_00062,
CC       ECO:0000256|SAAS:SAAS00366877}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and
CC       CysN. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00065}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. CysN/NodQ
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00062}.
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:KWX19922.1}.
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DR   EMBL; LGTW01000034; KWX19922.1; -; Genomic_DNA.
DR   RefSeq; WP_067858805.1; NZ_LGTW01000034.1.
DR   EnsemblBacteria; KWX19922; KWX19922; AFM11_33610.
DR   PATRIC; fig|59750.3.peg.5055; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000070612; Unassembled WGS sequence.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00455; apsK; 1.
DR   TIGRFAMs; TIGR02034; CysN; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00444459};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070612};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055993};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|SAAS:SAAS00774014};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055970};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056011, ECO:0000313|EMBL:KWX19922.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070612};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056018, ECO:0000313|EMBL:KWX19922.1}.
FT   DOMAIN        5    220       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      14     21       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND      91     95       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     146    149       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     455    462       ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
FT   ACT_SITE    529    529       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00065}.
SQ   SEQUENCE   619 AA;  68194 MW;  36A7C47B98098579 CRC64;
     MSDMATLLRI ATAGSVDDGK STLIGRLLYD SKAVMEDQLA AVERTSKERG NDYTDLALVT
     DGLRSEREQG ITIDVAYRYF ATAKRKFIIA DTPGHIQYTR NMVTGTSTAH LAIVLVDARH
     GLLEQSRRHA FLASLLGVQH IVLAVNKMDL IDWNQEKFND IRDEFHAFAA RLDIHDVTTI
     PMSALNGDNV VTKSDKAPWY DGPALLSHLE DVYIAGDRNL VDVRFPVQYV IRPQTVDHAD
     HRSYAGTVAS GVMRVGDEIV VLPSGKSSTI TAIDAPTGPV TEAFPPMAVS VSLADDIDIS
     RGDVLARVNN QPHVSTEFDA TVCWMADGSA LEPGREYLVK HTTRTTRARV ASLDYRLDVN
     TLHRDKSATA LKLNELGRIT LRSQQPLMLD EYSRNAATGA FILIDPDTNG TVAAGMVRDT
     TPVANRAASP NTVRHQSLVC ADDRLSKGRT IWFTGLSGSG KSSVAMRVEQ KLLERGCPAY
     VLDGDNLRHG LNADLGFSMA DRAENLRRLA HIATLMADSG LTVLVPAISP LTEHRELARA
     VHANQGFEFF EVFCDTPLED CERRDPKGLY KKARAGEITH FTGIDSPYQR PKNPDLRLVP
     DRDVDELADQ VIEMLDSRR
//
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