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

63 structures for P07329

Entry ID Method Resolution Chain Position Source
1FP4 X-ray 250 A B/D 1-523 PDB
1G20 X-ray 220 A B/D 1-523 PDB
1G21 X-ray 300 A B/D 1-523 PDB
1L5H X-ray 230 A B 2-523 PDB
1M1N X-ray 116 A B/D/F/H 2-523 PDB
1M1Y X-ray 320 A B/D/J/L 2-523 PDB
1M34 X-ray 230 A B/D/J/L 2-523 PDB
1N2C X-ray 300 A B/D 2-523 PDB
2AFH X-ray 210 A B/D 2-523 PDB
2AFI X-ray 310 A B/D/J/L 2-523 PDB
2MIN X-ray 203 A B/D 2-523 PDB
3K1A X-ray 223 A B/D 2-523 PDB
3MIN X-ray 203 A B/D 2-523 PDB
3U7Q X-ray 100 A B/D 1-523 PDB
4ND8 X-ray 200 A B/D 1-523 PDB
4TKU X-ray 143 A B/D 1-523 PDB
4TKV X-ray 150 A B/D 1-523 PDB
4WNA X-ray 200 A B/D 1-523 PDB
4WZA X-ray 190 A B/D 2-523 PDB
4WZB X-ray 230 A B/D 2-523 PDB
4XPI X-ray 197 A B/D 2-523 PDB
5BVG X-ray 160 A B/D 1-523 PDB
5BVH X-ray 153 A B/D 1-523 PDB
5CX1 X-ray 175 A B/D/F/H/J/L/N/P 1-523 PDB
5VQ4 X-ray 230 A B/D 1-523 PDB
6BBL X-ray 168 A B/D 1-523 PDB
6CDK X-ray 210 A B/D 1-523 PDB
6O7L X-ray 226 A B/D 1-523 PDB
6O7M X-ray 140 A B/D 1-523 PDB
6O7N X-ray 175 A B/D 1-523 PDB
6O7O X-ray 189 A B/D 1-523 PDB
6O7P X-ray 170 A B/D 1-523 PDB
6O7Q X-ray 200 A B/D 1-523 PDB
6O7R X-ray 227 A B/D 1-523 PDB
6O7S X-ray 227 A B/D 1-523 PDB
6OP1 X-ray 170 A B/D 2-523 PDB
6OP2 X-ray 190 A B/D 2-523 PDB
6OP3 X-ray 160 A B/D 2-523 PDB
6OP4 X-ray 230 A B/D 2-523 PDB
6UG0 X-ray 183 A B/D 1-523 PDB
6VXT X-ray 174 A B/D 1-523 PDB
7JRF X-ray 133 A B/D 1-523 PDB
7MCI X-ray 165 A B/D 1-523 PDB
7UT6 EM 191 A B/D 1-523 PDB
7UT7 EM 191 A B/D 1-523 PDB
7UT8 EM 243 A B/D 1-523 PDB
7UT9 EM 244 A B/D 1-523 PDB
7UTA EM 240 A B/D 1-523 PDB
8BTS X-ray 303 A B/D/I/L 1-523 PDB
8CRS EM 204 A B/D 2-523 PDB
8DBX EM 192 A B/D 1-523 PDB
8DBY EM 226 A B/D 1-523 PDB
8DFC EM 248 A B/D 1-523 PDB
8DFD EM 212 A B/D 1-523 PDB
8DPN EM 249 A B/D 1-523 PDB
8E3T X-ray 220 A B/D 1-523 PDB
8E3U X-ray 199 A B/D 1-523 PDB
8E3V X-ray 200 A B/D 1-523 PDB
8ENL EM 237 A B/D 2-523 PDB
8ENM EM 214 A B/D 1-523 PDB
8ENN EM 258 A B/D 2-523 PDB
8ENO EM 271 A B/D 2-523 PDB
AF-P07329-F1 Predicted AlphaFoldDB

No variants for P07329

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P07329

No associated diseases with P07329

4 regional properties for P07329

Type Name Position InterPro Accession
conserved_site Nitrogenase component 1, conserved site 88 - 95 IPR000318-1
conserved_site Nitrogenase component 1, conserved site 151 - 165 IPR000318-2
domain Nitrogenase/oxidoreductase, component 1 70 - 501 IPR000510
domain Nitrogenase molybdenum-iron protein beta chain, N-terminal 1 - 56 IPR024564

Functions

Description
EC Number 1.18.6.1 With dinitrogen 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
molybdenum-iron nitrogenase complex An enzyme complex containing a molybdenum-iron cluster found in many species. It is composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase, the molybdenum-iron protein, is tetrameric with an alpha2-beta2 structure, and nitrogenase reductase is a homodimer.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
carbonyl sulfide nitrogenase activity Catalysis of the reaction: carbonyl sulfide + 2 H+ + 2 e- = hydrogen sulfide + carbon monoxide.
iron-sulfur cluster binding Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
metal ion binding Binding to a metal ion.
nitrogenase activity Catalysis of the reaction: 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + 2 NH3 + 16 ADP + 16 phosphate.

1 GO annotations of biological process

Name Definition
nitrogen fixation The process in which nitrogen is taken from its relatively inert molecular form (N2) in the atmosphere and converted into nitrogen compounds useful for other chemical processes, such as ammonia, nitrate and nitrogen dioxide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQQVDKIKA SYPLFLDQDY KDMLAKKRDG FEEKYPQDKI DEVFQWTTTK EYQELNFQRE
70 80 90 100 110 120
ALTVNPAKAC QPLGAVLCAL GFEKTMPYVH GSQGCVAYFR SYFNRHFREP VSCVSDSMTE
130 140 150 160 170 180
DAAVFGGQQN MKDGLQNCKA TYKPDMIAVS TTCMAEVIGD DLNAFINNSK KEGFIPDEFP
190 200 210 220 230 240
VPFAHTPSFV GSHVTGWDNM FEGIARYFTL KSMDDKVVGS NKKINIVPGF ETYLGNFRVI
250 260 270 280 290 300
KRMLSEMGVG YSLLSDPEEV LDTPADGQFR MYAGGTTQEE MKDAPNALNT VLLQPWHLEK
310 320 330 340 350 360
TKKFVEGTWK HEVPKLNIPM GLDWTDEFLM KVSEISGQPI PASLTKERGR LVDMMTDSHT
370 380 390 400 410 420
WLHGKRFALW GDPDFVMGLV KFLLELGCEP VHILCHNGNK RWKKAVDAIL AASPYGKNAT
430 440 450 460 470 480
VYIGKDLWHL RSLVFTDKPD FMIGNSYGKF IQRDTLHKGK EFEVPLIRIG FPIFDRHHLH
490 500 510 520
RSTTLGYEGA MQILTTLVNS ILERLDEETR GMQATDYNHD LVR