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Database: UniProt
Entry: D9QSS6_ACEAZ
LinkDB: D9QSS6_ACEAZ
Original site: D9QSS6_ACEAZ 
ID   D9QSS6_ACEAZ            Unreviewed;       458 AA.
AC   D9QSS6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Sulfide dehydrogenase (Flavoprotein) subunit SudA {ECO:0000313|EMBL:ADL11614.1};
DE            EC=1.8.1.- {ECO:0000313|EMBL:ADL11614.1};
GN   OrderedLocusNames=Acear_0063 {ECO:0000313|EMBL:ADL11614.1};
OS   Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL11614.1, ECO:0000313|Proteomes:UP000001661};
RN   [1] {ECO:0000313|EMBL:ADL11614.1, ECO:0000313|Proteomes:UP000001661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC   {ECO:0000313|Proteomes:UP000001661};
RX   PubMed=21304692;
RA   Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA   Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT   7288).";
RL   Stand. Genomic Sci. 3:57-65(2010).
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DR   EMBL; CP002105; ADL11614.1; -; Genomic_DNA.
DR   RefSeq; WP_013277061.1; NC_014378.1.
DR   AlphaFoldDB; D9QSS6; -.
DR   STRING; 574087.Acear_0063; -.
DR   KEGG; aar:Acear_0063; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_000422_3_3_9; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000001661; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006004; SudA-like.
DR   NCBIfam; TIGR01316; gltA; 1.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADL11614.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001661}.
FT   DOMAIN          15..124
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          137..444
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   458 AA;  50148 MW;  FB1590093438DBF8 CRC64;
     MANRQKMKKQ QPEKRINNFQ EVACGYTKEE AVKEAERCLQ CKDSPCVDGC PVEVPIPDFI
     EEITNENFDQ AAELVKEKNA LPAICGRVCP QAEQCEAECI LGKKGQPVAI GALERFVGDY
     ELKQDREIEA KTDKDIKTAV VGSGPAGLTA AADMAKLGYQ VTVFEALSDP GGVLRYGIPE
     FRLPKSIVDE EVQEIENLGV EVRPNTLIGS TLTFDDLQEE GYEAVFVSTG AGLPYFLGIP
     GENLNGVYSA NEFLTRVNLM NAYRFPEYQT PIEVGDHVAV VGAGNVAMDS ARTALRLGAE
     EVSIVYRRSR NEMPAREEEI EHAEEEGIDF KLLRNPVKIL GNEEDWVAEL ECVEMELGEP
     DSSGRPRPIP IEDSNFTIPV ETVVIAIGQG PNPLLSKKEL NLETTEWNSI VVDDDTYQTS
     IPGVFAGGDV IGGSATVIAA MGDGRKAARE IDKYLQQK
//
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