APRA_MEGG1
ID APRA_MEGG1 Reviewed; 666 AA.
AC T2G6Z9; D2YW42; S5WDB4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Adenylylsulfate reductase subunit alpha {ECO:0000303|PubMed:19820092, ECO:0000303|PubMed:2158885, ECO:0000312|EMBL:AGS82785.1, ECO:0000312|EMBL:AGW12370.1, ECO:0000312|PDB:3GYX};
DE Short=AdoPSO(4) reductase subunit A {ECO:0000303|PubMed:2158885};
DE EC=1.8.99.2 {ECO:0000269|PubMed:19820092, ECO:0000269|PubMed:2158885, ECO:0000269|PubMed:7240092};
DE AltName: Full=Adenosine 5'-phosphosulfate reductase subunit alpha {ECO:0000303|PubMed:19820092};
DE Short=APSR subunit A {ECO:0000303|PubMed:19820092};
GN Name=aprA {ECO:0000303|PubMed:19820092, ECO:0000312|EMBL:AGS82785.1,
GN ECO:0000312|EMBL:AGW12370.1};
GN ORFNames=DGI_0457 {ECO:0000312|EMBL:AGW12370.1};
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448;
RN [1] {ECO:0000312|EMBL:AGS82785.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000312|EMBL:AGS82785.1};
RX PubMed=23974026; DOI=10.1128/jb.00411-13;
RA Morais-Silva F.O., Santos C.I., Rodrigues R., Pereira I.A.,
RA Rodrigues-Pousada C.;
RT "Roles of HynAB and Ech, the only two hydrogenases found in the model
RT sulfate reducer Desulfovibrio gigas.";
RL J. Bacteriol. 195:4753-4760(2013).
RN [2] {ECO:0000312|EMBL:AGW12370.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000312|EMBL:AGW12370.1};
RA Morais-Silva F.O., Rezende A.M., Pimentel C., Resende D.M., Santos C.I.,
RA Clemente C., de Oliveira L.M., da Silva S.M., Costa D.A., Varela-Raposo A.,
RA Horacio E.C.A., Matos M., Flores O., Ruiz J.C., Rodrigues-Pousada C.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|PDB:3GYX, ECO:0007744|PDB:3GYX}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-664, X-RAY CRYSTALLOGRAPHY (3.20
RP ANGSTROMS) IN COMPLEX WITH FAD AND APRB, FUNCTION, CATALYTIC ACTIVITY OF
RP THE ADENYLYLSULFATE REDUCTASE, COFACTOR, SUBUNIT, DOMAINS, AND SITES.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000303|PubMed:19820092};
RX PubMed=19820092; DOI=10.1128/jb.00583-09;
RA Chiang Y.L., Hsieh Y.C., Fang J.Y., Liu E.H., Huang Y.C., Chuankhayan P.,
RA Jeyakanthan J., Liu M.Y., Chan S.I., Chen C.J.;
RT "Crystal structure of Adenylylsulfate reductase from Desulfovibrio gigas
RT suggests a potential self-regulation mechanism involving the C terminus of
RT the beta-subunit.";
RL J. Bacteriol. 191:7597-7608(2009).
RN [4]
RP CATALYTIC ACTIVITY OF THE ADENYLYLSULFATE REDUCTASE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=7240092; DOI=10.1128/jb.147.1.161-169.1981;
RA Odom J.M., Peck H.D. Jr.;
RT "Localization of dehydrogenases, reductases, and electron transfer
RT components in the sulfate-reducing bacterium Desulfovibrio gigas.";
RL J. Bacteriol. 147:161-169(1981).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY OF THE ADENYLYLSULFATE REDUCTASE, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND EPR AND MOESSBAUER SPECTROSCOPY
RP OF THE ADENYLYLSULFATE REDUCTASE.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000303|PubMed:2158885};
RX PubMed=2158885; DOI=10.1111/j.1432-1033.1990.tb15447.x;
RA Lampreia J., Moura I., Teixeira M., Peck H.D. Jr., Legall J., Huynh B.H.,
RA Moura J.J.;
RT "The active centers of adenylylsulfate reductase from Desulfovibrio gigas.
RT Characterization and spectroscopic studies.";
RL Eur. J. Biochem. 188:653-664(1990).
CC -!- FUNCTION: Catalytic subunit of the adenylylsulfate reductase which
CC catalyzes reversibly the reduction of adenosine 5'-phosphosulfate (APS)
CC to sulfite and AMP during dissimilatory sulfate reduction.
CC {ECO:0000269|PubMed:19820092, ECO:0000269|PubMed:2158885}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + AMP + 2 H(+) + sulfite = adenosine 5'-phosphosulfate +
CC AH2; Xref=Rhea:RHEA:24240, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:58243,
CC ChEBI:CHEBI:456215; EC=1.8.99.2;
CC Evidence={ECO:0000269|PubMed:19820092, ECO:0000269|PubMed:2158885,
CC ECO:0000269|PubMed:7240092};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19820092, ECO:0000269|PubMed:2158885};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for sulfite {ECO:0000269|PubMed:2158885};
CC KM=0.16 mM for AMP {ECO:0000269|PubMed:2158885};
CC pH dependence:
CC Optimum pH is 7.4 for the adenylylsulfate reductase.
CC {ECO:0000269|PubMed:2158885};
CC -!- SUBUNIT: Heterodimer composed of AprA and AprB (PubMed:19820092,
CC PubMed:2158885). The heterodimers can dimerize to form heterotetramers
CC (PubMed:2158885). {ECO:0000269|PubMed:19820092,
CC ECO:0000269|PubMed:2158885}.
CC -!- INTERACTION:
CC T2G6Z9; T2G899: aprB; NbExp=3; IntAct=EBI-6409227, EBI-6409220;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7240092}.
CC -!- DOMAIN: Consists of three sections from the N- to the C-terminus: FAD-
CC binding domain, capping domain and helical domain. The FAD-binding
CC domain and the capping domain slightly overlap and form a channel that
CC may transport the substrate. {ECO:0000269|PubMed:19820092}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC {ECO:0000305}.
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DR EMBL; KF113859; AGS82785.1; -; Genomic_DNA.
DR EMBL; CP006585; AGW12370.1; -; Genomic_DNA.
DR RefSeq; WP_021759000.1; NZ_AUBO01000012.1.
DR PDB; 3GYX; X-ray; 3.20 A; A/C/E/G/I/K=3-663.
DR PDBsum; 3GYX; -.
DR AlphaFoldDB; T2G6Z9; -.
DR SMR; T2G6Z9; -.
DR IntAct; T2G6Z9; 1.
DR STRING; 1121448.DGI_0457; -.
DR PRIDE; T2G6Z9; -.
DR KEGG; dgg:DGI_0457; -.
DR PATRIC; fig|1121448.10.peg.454; -.
DR HOGENOM; CLU_014312_8_3_7; -.
DR OMA; GASSHKF; -.
DR SABIO-RK; T2G6Z9; -.
DR Proteomes; UP000016587; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009973; F:adenylyl-sulfate reductase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0019420; P:dissimilatory sulfate reduction; IDA:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR011803; AprA.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR PANTHER; PTHR11632:SF53; PTHR11632:SF53; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR02061; aprA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..666
FT /note="Adenylylsulfate reductase subunit alpha"
FT /id="PRO_0000434041"
FT BINDING 32..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092"
FT BINDING 60..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 67..69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092"
FT BINDING 78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092"
FT BINDING 193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092"
FT BINDING 259
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 417
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 461..462
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 472
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT SITE 160
FT /note="Important for interaction with AprB and for the
FT recognition of substrate at the substrate channel entrance"
FT /evidence="ECO:0000269|PubMed:19820092"
FT SITE 282
FT /note="Important for interaction with AprB and for the
FT binding of substrate at the substrate channel entrance"
FT /evidence="ECO:0000269|PubMed:19820092"
FT SITE 300
FT /note="Important for interaction with AprB and for the
FT binding of substrate at the substrate channel entrance"
FT /evidence="ECO:0000269|PubMed:19820092"
FT CONFLICT 664
FT /note="T -> D (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 34..50
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 103..123
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 205..217
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 338..345
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 387..395
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 471..492
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 504..511
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 537..551
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 555..559
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 563..579
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 588..613
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 646..649
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 650..656
FT /evidence="ECO:0007829|PDB:3GYX"
SQ SEQUENCE 666 AA; 74880 MW; 7FD12237BFBF6FBC CRC64;
MPKIPSKETP RGVAIAEPII VEHSVDLLMV GGGMGNCGAA FEAVRWADKY APEAKILLVD
KASLERSGAV AQGLSAINTY LGDNNADDYV RMVRTDLMGL VREDLIYDLG RHVDDSVHLF
EEWGLPVWIK DEHGHNLDGA QAKAAGKSLR NGDKPVRSGR WQIMINGESY KVIVAEAAKN
ALGQDRIIER IFIVKLLLDK NTPNRIAGAV GFNLRANEVH IFKANAMVVA CGGAVNVYRP
RSVGEGMGRA WYPVWNAGST YTMCAQVGAE MTMMENRFVP ARFKDGYGPV GAWFLLFKAK
ATNCKGEDYC ATNRAMLKPY EERGYAKGHV IPTCLRNHMM LREMREGRGP IYMDTKTALQ
TSFATMSPAQ QKHLEAEAWE DFLDMCVGQA NLWAATNCAP EERGSEIMPT EPYLLGSHSG
CCGIWASGPD EAWVPEDYKV RAANGKVYNR MTTVEGLWTC ADGVGASGHK FSSGSHAEGR
IVGKQMVRWY LDHKDFKPEF VETAEELKTL IYRPYYNYEK GKGASTCPVV NPEYISPKNF
MMRLIKCTDE YGGGVGTYYN TSKALLDTGF WLMEMLEEDS LKLAARDLHE LLRCWENYHR
LWTVRLHMQH IAFREESRYP GFYYRADFLG LDDSKWKCFV NSKYDPAKKE TKIFKKPYYQ
IIPTDA
