Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

20 structures for P17846

Entry ID Method Resolution Chain Position Source
1AOP X-ray 160 A A 74-570 PDB
2AOP X-ray 175 A A 74-570 PDB
2GEP X-ray 190 A A 74-570 PDB
3AOP X-ray 210 A A 74-570 PDB
3GEO X-ray 210 A A 74-570 PDB
4AOP X-ray 180 A A 74-570 PDB
4G38 X-ray 156 A A 1-570 PDB
4G39 X-ray 240 A A 1-570 PDB
4GEP X-ray 200 A A 74-570 PDB
4HTR X-ray 160 A A 64-570 PDB
5AOP X-ray 220 A A 74-570 PDB
5GEP X-ray 210 A A 74-570 PDB
6C3M X-ray 150 A A 1-570 PDB
6C3X X-ray 154 A A 1-570 PDB
6C3Y X-ray 154 A A 1-570 PDB
6C3Z X-ray 168 A A 1-570 PDB
6GEP X-ray 180 A A 74-570 PDB
7GEP X-ray 240 A A 74-570 PDB
8GEP X-ray 220 A A 74-570 PDB
AF-P17846-F1 Predicted AlphaFoldDB

No variants for P17846

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P17846

No associated diseases with P17846

2 regional properties for P17846

Type Name Position InterPro Accession
binding_site Cysteine synthase/cystathionine beta-synthase, pyridoxal-phosphate attachment site 35 - 53 IPR001216
domain Tryptophan synthase beta chain-like, PALP domain 9 - 294 IPR001926

Functions

Description
EC Number 1.8.1.2 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
sulfite reductase complex (NADPH) A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide.

7 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
sulfite reductase (ferredoxin) activity Catalysis of the reaction: hydrogen sulfide + 3 oxidized ferredoxin + 3 H2O = sulfite + 3 reduced ferredoxin.
sulfite reductase (NADPH) activity Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+.
sulfite reductase activity Catalysis of the reaction: hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor.

3 GO annotations of biological process

Name Definition
cysteine biosynthetic process The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid.
hydrogen sulfide biosynthetic process The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.
sulfate assimilation The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ
70 80 90 100 110 120
DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID KFAGENTIYG SIRLTNRQTF
130 140 150 160 170 180
QFHGILKKNV KPVHQMLHSV GLDALATAND MNRNVLCTSN PYESQLHAEA YEWAKKISEH
190 200 210 220 230 240
LLPRTRAYAE IWLDQEKVAT TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI
250 260 270 280 290 300
AENGKLVGFN LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT
310 320 330 340 350 360
DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK GIDDNWHLTL
370 380 390 400 410 420
FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII AGVPESEKAK IEKIAKESGL
430 440 450 460 470 480
MNAVTPQREN SMACVSFPTC PLAMAEAERF LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP
490 500 510 520 530 540
NGCGRAMLAE VGLVGKAPGR YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK
550 560
EREAGEGFGD FTVRAGIIRP VLDPARDLWD