ID A0A081G0C3_9GAMM Unreviewed; 473 AA.
AC A0A081G0C3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|HAMAP-Rule:MF_02095};
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};
DE Includes:
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ {ECO:0000256|HAMAP-Rule:MF_02095};
DE EC=3.1.3.7 {ECO:0000256|HAMAP-Rule:MF_02095};
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_02095};
DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_02095};
DE Short=PAP phosphatase {ECO:0000256|HAMAP-Rule:MF_02095};
GN Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN Synonyms=cysQ {ECO:0000256|HAMAP-Rule:MF_02095};
GN ORFNames=ADIMK_1474 {ECO:0000313|EMBL:KEA64228.1};
OS Marinobacterium lacunae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA64228.1, ECO:0000313|Proteomes:UP000028252};
RN [1] {ECO:0000313|EMBL:KEA64228.1, ECO:0000313|Proteomes:UP000028252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK27 {ECO:0000313|EMBL:KEA64228.1,
RC ECO:0000313|Proteomes:UP000028252};
RA Singh A., Pinnaka A.K.;
RT "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT collected from Kochi backwaters in Kerala, India.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|ARBA:ARBA00002632, ECO:0000256|HAMAP-Rule:MF_00065}.
CC -!- FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
CC {ECO:0000256|HAMAP-Rule:MF_02095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001823, ECO:0000256|HAMAP-
CC Rule:MF_00065};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02095};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000256|ARBA:ARBA00004806, ECO:0000256|HAMAP-
CC Rule:MF_00065}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02095}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02095}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02095}.
CC -!- SIMILARITY: Belongs to the APS kinase family.
CC {ECO:0000256|ARBA:ARBA00007008, ECO:0000256|HAMAP-Rule:MF_00065}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CysQ
CC family. {ECO:0000256|ARBA:ARBA00005289, ECO:0000256|HAMAP-
CC Rule:MF_02095}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEA64228.1}.
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DR EMBL; JMQN01000018; KEA64228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081G0C3; -.
DR STRING; 1232683.ADIMK_1474; -.
DR PATRIC; fig|1232683.4.peg.1453; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG1218; Bacteria.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000028252; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd02027; APSK; 1.
DR CDD; cd01638; CysQ; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR HAMAP; MF_02095; CysQ; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR006240; CysQ.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00455; apsK; 1.
DR NCBIfam; TIGR01331; bisphos_cysQ; 1.
DR PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00065};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_02095};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02095};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02095, ECO:0000313|EMBL:KEA64228.1};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_02095};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02095};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02095};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00065}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW Reference proteome {ECO:0000313|Proteomes:UP000028252};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT ACT_SITE 384
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02095"
FT BINDING 310..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 473 AA; 52389 MW; 47B5485566AF19F9 CRC64;
MPDLQAIIEI ARQAGEKIMA IYAQDFAVYD KSDSSPLTEA DLASHHCIIE GLKKLTPEIP
ILSEESSKSD IDDRMSWSCY WLIDPLDGTK EFIKKNGEFT VNIALIDNHK PVLGVVHVPA
KGVTYYGECG QGAFKTEGGV TQPIKVKALP SEGETWQVVG SRSHQSDEFR EFIDTLPNAE
IVSMGSSLKL CLVAEGEADL YPRLGPTSEW DTAAAQAVVE AAGGLVLAFP SLEPMRYNTR
SDTLLNPWFM VCAAVSEVWA SGRTHQPKGA QYEFRDHDSQ AQVVWNHTSV TPEVRAKQKN
QHPRCIWFTG LSGSGKSTLA NALEKALVEK GYHTMLLDGD NVRHGLCKDL GMSEADRTEN
IRRVGELAKL MTEAGLIVIT AFISPFRADR EAARALFDDG DFIEVYVEAP LEVCEQRDPK
GLYERARKGE IRDFTGVDSP YQKPVIPEII ANTSKYDVIS IIKNIYRAIT SEY
//
